EC |
1.1.1.101 |
Accepted name: |
acylglycerone-phosphate reductase |
Reaction: |
1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+ |
Other name(s): |
palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase |
Systematic name: |
1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase |
Comments: |
Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-35-4 |
References: |
1. |
LaBelle, E.F., Jr. and Hajira, A.K. Enzymatic reduction of alkyl and acyl derivatives of dihydroxyacetone phosphate by reduced pyridine nucleotides. J. Biol. Chem. 247 (1972) 5825–5834. [PMID: 4403490] |
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[EC 1.1.1.101 created 1972, modified 1976] |
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EC |
1.1.1.102 |
Accepted name: |
3-dehydrosphinganine reductase |
Reaction: |
sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+ |
Other name(s): |
D-3-dehydrosphinganine reductase; D-3-oxosphinganine reductase; DSR; 3-oxosphinganine reductase; 3-oxosphinganine:NADPH oxidoreductase; D-3-oxosphinganine:B-NADPH oxidoreductase |
Systematic name: |
D-erythro-dihydrosphingosine:NADP+ 3-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-36-5 |
References: |
1. |
Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664–670. [PMID: 4386961] |
2. |
Stoffel, W., Le Kim, D. and Sticht, G. Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one). Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1637–1644. [PMID: 4387676] |
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[EC 1.1.1.102 created 1972] |
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EC |
1.1.1.103 |
Accepted name: |
L-threonine 3-dehydrogenase |
Reaction: |
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ |
Other name(s): |
L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; TDH |
Systematic name: |
L-threonine:NAD+ oxidoreductase |
Comments: |
This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-99-6 |
References: |
1. |
Green, M.L. and Elliott, W.H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem. J. 92 (1964) 537–549. [PMID: 4284408] |
2. |
Hartshorne, D. and Greenberg, D.M. Studies on liver threonine dehydrogenase. Arch. Biochem. Biophys. 105 (1964) 173–178. [DOI] [PMID: 14165492] |
3. |
Newman, E.B., Kapoor, V. and Potter, R. Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli. J. Bacteriol. 126 (1976) 1245–1249. [PMID: 7548] |
4. |
Epperly, B.R. and Dekker, E.E. L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 (1991) 6086–6092. [PMID: 2007567] |
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[EC 1.1.1.103 created 1972] |
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EC |
1.1.1.104 |
Accepted name: |
4-oxoproline reductase |
Reaction: |
cis-4-hydroxy-L-proline + NAD+ = 4-oxo-L-proline + NADH + H+ |
Other name(s): |
cis-hydroxy-L-proline oxidase |
Systematic name: |
cis-4-hydroxy-L-proline:NAD+ oxidoreductase (4-oxo-L-proline forming) |
Comments: |
The enzyme, isolated from animals, is specific for 4-oxo-L-proline and cis-4-hydroxy-L-proline. It has no activity with trans-4-hydroxy-L-proline. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-37-6 |
References: |
1. |
Smith, T.E. and Mitoma, C. Partial purification and some properties of 4-ketoproline reductase. J. Biol. Chem. 237 (1962) 1177–1180. [PMID: 13914427] |
2. |
Kwiatkowski, S., Bozko, M., Zarod, M., Witecka, A., Kocdemir, K., Jagielski, A.K. and Drozak, J. Recharacterization of the mammalian cytosolic type 2 (R)-β-hydroxybutyrate dehydrogenase (BDH2) as 4-oxo-L-proline reductase (EC 1.1.1.104). J. Biol. Chem. 298:101708 (2022). [DOI] [PMID: 35150746] |
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[EC 1.1.1.104 created 1972, modified 2022] |
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EC |
1.1.1.105 |
Accepted name: |
all-trans-retinol dehydrogenase (NAD+) |
Reaction: |
all-trans-retinol—[cellular-retinol-binding-protein] + NAD+ = all-trans-retinal—[cellular-retinol-binding-protein] + NADH + H+ |
|
For diagram of retinal and derivatives biosynthesis, click here |
Other name(s): |
retinol (vitamin A1) dehydrogenase; MDR; microsomal retinol dehydrogenase; retinol dehydrogenase (misleading); retinal reductase (ambiguous); retinene reductase; epidermal retinol dehydrogenase 2; SDR16C5 (gene name); RDH16 (gene name) |
Systematic name: |
all-trans retinol:NAD+ oxidoreductase |
Comments: |
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3α-hydroxysteroids [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-53-8 |
References: |
1. |
Koen, A.L. and Shaw, C.R. Retinol and alcohol dehydrogenases in retina and liver. Biochim. Biophys. Acta 128 (1966) 48–54. [PMID: 5972368] |
2. |
Gough, W.H., VanOoteghem, S., Sint, T. and Kedishvili, N.Y. cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids. J. Biol. Chem. 273 (1998) 19778–19785. [DOI] [PMID: 9677409] |
3. |
Matsuzaka, Y., Okamoto, K., Tsuji, H., Mabuchi, T., Ozawa, A., Tamiya, G. and Inoko, H. Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion. Biochem. Biophys. Res. Commun. 297 (2002) 1171–1180. [DOI] [PMID: 12372410] |
4. |
Lee, S.A., Belyaeva, O.V. and Kedishvili, N.Y. Biochemical characterization of human epidermal retinol dehydrogenase 2. Chem. Biol. Interact. 178 (2009) 182–187. [DOI] [PMID: 18926804] |
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[EC 1.1.1.105 created 1972, modified 2011] |
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EC |
1.1.1.106 |
Accepted name: |
pantoate 4-dehydrogenase |
Reaction: |
(R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+ |
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For diagram of pantothenate catabolism, click here |
Glossary: |
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate |
Other name(s): |
pantoate dehydrogenase; pantothenase; D-pantoate:NAD+ 4-oxidoreductase |
Systematic name: |
(R)-pantoate:NAD+ 4-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-38-7 |
References: |
1. |
Goodhue, C.T. and Snell, E.E. The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid. Biochemistry 5 (1966) 403–408. [PMID: 4287370] |
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[EC 1.1.1.106 created 1972, modified 1976] |
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EC |
1.1.1.107 |
Accepted name: |
pyridoxal 4-dehydrogenase |
Reaction: |
pyridoxal + NAD+ = 4-pyridoxolactone + NADH + H+ |
Other name(s): |
pyridoxal dehydrogenase |
Systematic name: |
pyridoxal:NAD+ 4-oxidoreductase |
Comments: |
The enzyme acts on the hemiacetal form of the substrate. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-39-8 |
References: |
1. |
Burg, R.W. and Snell, E.E. The bacterial oxidation of vitamin B6. VI. Pyridoxal dehydrogenase and 4-pyridoxolactonase. J. Biol. Chem. 244 (1969) 2585–2589. [PMID: 4306030] |
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[EC 1.1.1.107 created 1972] |
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EC |
1.1.1.108 |
Accepted name: |
carnitine 3-dehydrogenase |
Reaction: |
carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+ |
Systematic name: |
carnitine:NAD+ 3-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9045-45-8 |
References: |
1. |
Aurich, H., Kleber, H.-P., Sorger, H. and Tauchert, H. Reinigung und Eigenschaften der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 6 (1968) 196–201. [DOI] [PMID: 4302217] |
2. |
Schöpp, W., Sorger, H., Kleber, H.-P. and Aurich, H. Kinetische Untersuchungen zum Reaktionmechanisms der Carnitindehydrogenase aus Pseudomonas aeruginosa. Eur. J. Biochem. 10 (1969) 56–60. [DOI] [PMID: 4310279] |
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[EC 1.1.1.108 created 1972] |
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EC
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1.1.1.109
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Transferred entry: | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. Now EC 1.3.1.28, 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
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[EC 1.1.1.109 created 1972, deleted 1976] |
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EC |
1.1.1.110 |
Accepted name: |
aromatic 2-oxoacid reductase |
Reaction: |
(1) (R)-3-(phenyl)lactate + NAD+ = 3-phenylpyruvate + NADH + H+ (2) (R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+ (3) (R)-(indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+ |
Glossary: |
3-phenylpyruvate = 2-oxo-3-phenylpropanoate |
Other name(s): |
(R)-aromatic lactate dehydrogenase; (R)-4-hydroxyphenyllactate dehydrogenase; indolelactate:NAD+ oxidoreductase; indolelactate dehydrogenase; fldH (gene name); (indol-3-yl)lactate:NAD+ oxidoreductase |
Systematic name: |
aromatic 2-oxoacid:NAD+ oxidoreductase |
Comments: |
The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-41-2 |
References: |
1. |
Jean, M. and DeMoss, R.D. Indolelactate dehydrogenase from Clostridium sporogenes. Can. J. Microbiol. 14 (1968) 429–435. [PMID: 4384683] |
2. |
Giesel, H. and Simon, H. On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius. Arch. Microbiol. 135 (1983) 51–57. [PMID: 6354130] |
3. |
Bode, R., Lippoldt, A. and Birnbaum, D. Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa. Biochem. Physiol. Pflanzen 181 (1986) 189–198. |
4. |
Dickert, S., Pierik, A.J., Linder, D. and Buckel, W. The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. Eur. J. Biochem. 267 (2000) 3874–3884. [DOI] [PMID: 10849007] |
5. |
Dodd, D., Spitzer, M.H., Van Treuren, W., Merrill, B.D., Hryckowian, A.J., Higginbottom, S.K., Le, A., Cowan, T.M., Nolan, G.P., Fischbach, M.A. and Sonnenburg, J.L. A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites. Nature 551 (2017) 648–652. [PMID: 29168502] |
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[EC 1.1.1.110 created 1972 (EC 1.1.1.222 created 2000, incorporated 2018), modified 2018] |
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EC |
1.1.1.111 |
Accepted name: |
3-(imidazol-5-yl)lactate dehydrogenase |
Reaction: |
(S)-3-(imidazol-5-yl)lactate + NAD(P)+ = 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+ |
Other name(s): |
imidazol-5-yl lactate dehydrogenase |
Systematic name: |
(S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-42-3 |
References: |
1. |
Coote, J.G. and Hassall, H. The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans. Biochem. J. 111 (1969) 237–239. [PMID: 4303364] |
2. |
Cortese, R., Brevet, J., Hedegaard, J. and Roche, J. [Identification and purification of an α-ketoacid aromatic reductase of Escherichia coli B] C.R. Seances Soc. Biol. Fil. 162 (1968) 390–395. [PMID: 4237631] (in French) |
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[EC 1.1.1.111 created 1972] |
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EC |
1.1.1.112 |
Accepted name: |
indanol dehydrogenase |
Reaction: |
indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+ |
Systematic name: |
indan-1-ol:NAD(P)+ 1-oxidoreductase |
Comments: |
3(20)α-Hydroxysteroids are also oxidized, more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-43-4 |
References: |
1. |
Billings, R.E., Sullivan, H.R. and McMahon, R.E. The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver. J. Biol. Chem. 246 (1971) 3512–3517. [PMID: 4397102] |
2. |
Hara, A., Nakagawa, M., Taniguchi, H. and Sawada, H. 3(20)α-Hydroxysteroid dehydrogenase activity of monkey liver indanol dehydrogenase. J. Biochem. (Tokyo) 106 (1989) 900–903. [PMID: 2559080] |
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[EC 1.1.1.112 created 1972] |
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EC |
1.1.1.113 |
Accepted name: |
L-xylose 1-dehydrogenase |
Reaction: |
L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+ |
Other name(s): |
L-xylose dehydrogenase; NADPH-xylose reductase |
Systematic name: |
L-xylose:NADP+ 1-oxidoreductase |
Comments: |
Also oxidizes D-arabinose and D-lyxose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-44-5 |
References: |
1. |
Uehara, K. and Takeda, M. L-Xylose dehydrogenase in bakers' yeast. J. Biochem. (Tokyo) 52 (1962) 461–463. [PMID: 13995171] |
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[EC 1.1.1.113 created 1972] |
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EC |
1.1.1.114 |
Accepted name: |
apiose 1-reductase |
Reaction: |
D-apiitol + NAD+ = D-apiose + NADH + H+ |
Other name(s): |
D-apiose reductase; D-apiitol reductase |
Systematic name: |
D-apiitol:NAD+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-45-6 |
References: |
1. |
Hanna, R., Picken, M. and Mendicino, J. Purification of a specific D-apiitol dehydrogenase from a Micrococcus isolated from the surface of germinating parsley seeds. Biochim. Biophys. Acta 315 (1973) 259–271. |
2. |
Neal, D.L. and Kindel, P.K. D-Apiose reductase from Aerobacter aerogenes. J. Bacteriol. 101 (1970) 910–915. [PMID: 4314545] |
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[EC 1.1.1.114 created 1972] |
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EC |
1.1.1.115 |
Accepted name: |
ribose 1-dehydrogenase (NADP+) |
Reaction: |
D-ribose + NADP+ + H2O = D-ribonate + NADPH + H+ |
Other name(s): |
D-ribose dehydrogenase (NADP+); NADP-pentose-dehydrogenase; ribose 1-dehydrogenase (NADP) |
Systematic name: |
D-ribose:NADP+ 1-oxidoreductase |
Comments: |
Also acts, more slowly, on D-xylose and other pentoses. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-46-7 |
References: |
1. |
Scher, B.M. and Horecker, B.L. Pentose metabolism in Candida. 3. The triphosphopyridine nucleotide-specific polyol dehydrogenase of Candida utilis. Arch. Biochem. Biophys. 116 (1966) 117–128. [PMID: 4381350] |
2. |
Schiwara, H.W., Domschke, W. and Domagk, G.F. Über die Zucker-Dehydrogenase in der Säugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575–1581. [PMID: 4393642] |
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[EC 1.1.1.115 created 1972] |
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EC |
1.1.1.116 |
Accepted name: |
D-arabinose 1-dehydrogenase (NAD+) |
Reaction: |
D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+ |
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For diagram of D-arabinose catabolism, click here |
Other name(s): |
NAD+-pentose-dehydrogenase; arabinose(fucose)dehydrogenase |
Systematic name: |
D-arabinose:NAD+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-47-8 |
References: |
1. |
Palleroni, N.J. and Doudoroff, M. Metabolism of carbohydrates by Pseudomonas saccharophilla. III. Oxidation of D-arabinose. J. Bacteriol. 74 (1957) 180–185. [PMID: 13475218] |
2. |
Schiwara, H.W., Domschke, W. and Domagk, G.F. Über die Zucker-Dehydrogenase in der Säugetierleber. I. Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustausch-chromatographie. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1575–1581. [PMID: 4393642] |
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[EC 1.1.1.116 created 1972] |
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EC |
1.1.1.117 |
Accepted name: |
D-arabinose 1-dehydrogenase [NAD(P)+] |
Reaction: |
D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+ |
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For diagram of D-arabinose catabolism, click here |
Other name(s): |
D-arabinose 1-dehydrogenase [NAD(P)] |
Systematic name: |
D-arabinose:NAD(P)+ 1-oxidoreductase |
Comments: |
Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-48-9 |
References: |
1. |
Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847] |
2. |
Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848] |
3. |
Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849] |
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[EC 1.1.1.117 created 1972] |
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EC |
1.1.1.118 |
Accepted name: |
glucose 1-dehydrogenase (NAD+) |
Reaction: |
D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+ |
Other name(s): |
D-glucose:NAD oxidoreductase; D-aldohexose dehydrogenase; glucose 1-dehydrogenase (NAD) |
Systematic name: |
D-glucose:NAD+ 1-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-49-0 |
References: |
1. |
Hu, A.S.L. and Cline, A.L. The regulation of some sugar dehydrogenases in a pseudomonad. Biochim. Biophys. Acta 93 (1964) 237–245. [DOI] [PMID: 14251301] |
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[EC 1.1.1.118 created 1972, modified 1976] |
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EC |
1.1.1.119 |
Accepted name: |
glucose 1-dehydrogenase (NADP+) |
Reaction: |
D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+ |
Other name(s): |
nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase; NADP-linked aldohexose dehydrogenase; NADP-dependent glucose dehydrogenase; glucose 1-dehydrogenase (NADP) |
Systematic name: |
D-glucose:NADP+ 1-oxidoreductase |
Comments: |
Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D-mannose. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-50-3 |
References: |
1. |
Adachi, O. and Ameyama, M. D-Glucose dehydrogenase from Gluconobacter suboxydans. Methods Enzymol. 89 (1982) 159–163. |
2. |
Avigad, G., Alroy, Y. and Englard, S. Purification and properties of a nicotinamide adenine dinucleotide phosphate-linked aldohexose dehydrogenase from Gluconobacter cerinus. J. Biol. Chem. 243 (1968) 1936–1941. [PMID: 4384672] |
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[EC 1.1.1.119 created 1972] |
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EC |
1.1.1.120 |
Accepted name: |
galactose 1-dehydrogenase (NADP+) |
Reaction: |
D-galactose + NADP+ = D-galactono-1,5-lactone + NADPH + H+ |
Other name(s): |
D-galactose dehydrogenase (NADP+); galactose 1-dehydrogenase (NADP) |
Systematic name: |
D-galactose:NADP+ 1-oxidoreductase |
Comments: |
Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-51-4 |
References: |
1. |
Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847] |
2. |
Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848] |
3. |
Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849] |
4. |
Schiwara, H.W. and Domagk, G.F. Über den Abbau der Desoxyzucker durch Bakterienenzyme. V. Anreicherung und Charakterisierung einer NADP-abhängigen Abequosedehydrogenase aus Pseudomonas putida. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 1321–1329. [PMID: 4387016] |
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[EC 1.1.1.120 created 1972] |
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EC |
1.1.1.121 |
Accepted name: |
aldose 1-dehydrogenase (NAD+) |
Reaction: |
D-aldose + NAD+ = D-aldonolactone + NADH + H+ |
Other name(s): |
aldose dehydrogenase; D-aldohexose dehydrogenase; aldose 1-dehydrogenase |
Systematic name: |
D-aldose:NAD+ 1-oxidoreductase |
Comments: |
Acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-61-3 |
References: |
1. |
Cline, A.L. and Hu, A.S.L. The isolation of three sugar dehydrogenases from a psuedomonad. J. Biol. Chem. 240 (1965) 4488–4492. [PMID: 5845847] |
2. |
Cline, A.L. and Hu, A.S.L. Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4493–4497. [PMID: 5845848] |
3. |
Cline, A.L. and Hu, A.S.L. Some physical properties of three sugar dehydrogenases from a pseudomonad. J. Biol. Chem. 240 (1965) 4498–4502. [PMID: 5845849] |
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[EC 1.1.1.121 created 1972] |
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EC |
1.1.1.122 |
Accepted name: |
D-threo-aldose 1-dehydrogenase |
Reaction: |
a D-threo-aldose + NAD+ = a D-threo-aldono-1,5-lactone + NADH + H+ |
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For diagram of L-fucose catabolism, click here |
Other name(s): |
L-fucose dehydrogenase; (2S,3R)-aldose dehydrogenase; dehydrogenase, L-fucose; L-fucose (D-arabinose) dehydrogenase |
Systematic name: |
D-threo-aldose:NAD+ 1-oxidoreductase |
Comments: |
Acts on L-fucose, D-arabinose and L-xylose; the animal enzyme was also shown to act on L-arabinose, and the enzyme from Pseudomonas caryophylli on L-glucose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9082-70-6 |
References: |
1. |
Sasajima, K.-I. and Sinskey, A.J. Oxidation of L-glucose by a Pseudomonad. Biochim. Biophys. Acta 571 (1979) 120–126. [DOI] [PMID: 40609] |
2. |
Schachter, H., Sarney, J., McGuire, E.J. and Roseman, S. Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver. J. Biol. Chem. 244 (1969) 4785–4792. [PMID: 4309152] |
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[EC 1.1.1.122 created 1972] |
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EC |
1.1.1.123 |
Accepted name: |
sorbose 5-dehydrogenase (NADP+) |
Reaction: |
L-sorbose + NADP+ = 5-dehydro-D-fructose + NADPH + H+ |
Other name(s): |
5-ketofructose reductase; 5-keto-D-fructose reductase; sorbose (nicotinamide adenine dinucleotide phosphate) dehydrogenase; reduced nicotinamide adenine dinucleotide phosphate-linked reductase; sorbose 5-dehydrogenase (NADP+) |
Systematic name: |
L-sorbose:NADP+ 5-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-52-5 |
References: |
1. |
Englard, S., Kaysen, G. and Avigad, G. 5-keto-D-Fructose. VI. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from yeast. J. Biol. Chem. 245 (1970) 1311–1318. [PMID: 4392628] |
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[EC 1.1.1.123 created 1972, modified 1976] |
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EC |
1.1.1.124 |
Accepted name: |
fructose 5-dehydrogenase (NADP+) |
Reaction: |
D-fructose + NADP+ = 5-dehydro-D-fructose + NADPH + H+ |
Other name(s): |
5-ketofructose reductase (NADP); 5-keto-D-fructose reductase (NADP+); fructose 5-(nicotinamide adenine dinucleotide phosphate) dehydrogenase; D-(-)fructose:(NADP+) 5-oxidoreductase; fructose 5-dehydrogenase (NADP) |
Systematic name: |
D-fructose:NADP+ 5-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-53-6 |
References: |
1. |
Ameyama, M., Matsushita, K., Shinagawa, E. and Adachi, O. 5-keto-D-Fructose reductase of Gluconobacter industrius. Purification, crystallization and properties. Agric. Biol. Chem. 45 (1981) 863–869. |
2. |
Avigad, G., Englard, S. and Pifco, S. 5-keto-D-Fructose. IV. A specific reduced nicotinamide adenine dinucleotide phosphate-linked reductase from Gluconobacter cerinus. J. Biol. Chem. 241 (1966) 373–378. [PMID: 4379259] |
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[EC 1.1.1.124 created 1972, modified 1976] |
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EC |
1.1.1.125 |
Accepted name: |
2-deoxy-D-gluconate 3-dehydrogenase |
Reaction: |
2-deoxy-D-gluconate + NAD+ = 3-dehydro-2-deoxy-D-gluconate + NADH + H+ |
Other name(s): |
2-deoxygluconate dehydrogenase |
Systematic name: |
2-deoxy-D-gluconate:NAD+ 3-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-54-7 |
References: |
1. |
Eichhorn, M.M. and Cynkin, M.A. Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid dehydrogenase. Biochemistry 4 (1965) 159–165. [PMID: 14285233] |
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[EC 1.1.1.125 created 1972] |
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EC |
1.1.1.126 |
Accepted name: |
2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase |
Reaction: |
2-dehydro-3-deoxy-D-gluconate + NADP+ = (4S,5S)-4,5-dihydroxy-2,6-dioxohexanoate + NADPH + H+ |
Other name(s): |
2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate dehydrogenase (ambiguous) |
Systematic name: |
2-dehydro-3-deoxy-D-gluconate:NADP+ 6-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-55-8 |
References: |
1. |
Preiss, J. and Ashwell, G. Alginic acid metabolism in bacteria. II. The enzymatic reduction of 4-deoxy-L-erythro-5-hexoseulose uronic acid to 2-keto-3-deoxy-D-gluconic acid. J. Biol. Chem. 237 (1962) 317–321. [PMID: 14488585] |
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[EC 1.1.1.126 created 1972] |
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EC |
1.1.1.127 |
Accepted name: |
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase |
Reaction: |
2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+ |
Other name(s): |
2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase (ambiguous); 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase (ambiguous) |
Systematic name: |
2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase |
Comments: |
The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-56-9 |
References: |
1. |
Condemine, G., Hugouvieux-Cotte-Pattat, N. and Robert-Baudouy, J. An enzyme in the pectolytic pathway of Erwinia chrysanthemi: 3-keto-3-deoxygluconate oxidoreductase. J. Gen. Microbiol. 130 (1984) 2839–2844. |
2. |
Preiss, J. and Ashwell, G. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid. J. Biol. Chem. 238 (1963) 1577–1583. [PMID: 13986017] |
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[EC 1.1.1.127 created 1972, modified 1976, modified 1989] |
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EC
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1.1.1.128
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Deleted entry: | L-idonate 2-dehydrogenase. The reaction described is covered by EC 1.1.1.264. |
[EC 1.1.1.128 created 1972, modified 1976, deleted 2012] |
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EC |
1.1.1.129 |
Accepted name: |
L-threonate 3-dehydrogenase |
Reaction: |
L-threonate + NAD+ = 3-dehydro-L-erythronate + NADH + H+ |
Other name(s): |
threonate dehydrogenase; L-threonic acid dehydrogenase |
Systematic name: |
L-threonate:NAD+ 3-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-59-2 |
References: |
1. |
Aspen, A.J. and Jakoby, W.B. L-Threonic acid dehydrogenase: purification and properties. J. Biol. Chem. 239 (1964) 710–713. [PMID: 14154441] |
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[EC 1.1.1.129 created 1972] |
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EC |
1.1.1.130 |
Accepted name: |
3-dehydro-L-gulonate 2-dehydrogenase |
Reaction: |
3-dehydro-L-gulonate + NAD(P)+ = (4R,5S)-4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H + H+ |
Other name(s): |
3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase; 3-keto-L-gulonate dehydrogenase; 3-ketogulonate dehydrogenase |
Systematic name: |
3-dehydro-L-gulonate:NAD(P)+ 2-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-61-6 |
References: |
1. |
Volk, W.A. and Larsen, J.L. β-Keto-L-gulonic acid as an intermediate in the bacterial metabolism of ascorbic acid. J. Biol. Chem. 237 (1962) 2454–2457. [PMID: 13926592] |
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[EC 1.1.1.130 created 1972] |
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EC |
1.1.1.131 |
Accepted name: |
mannuronate reductase |
Reaction: |
D-mannonate + NAD(P)+ = D-mannuronate + NAD(P)H + H+ |
Other name(s): |
mannonate dehydrogenase; mannonate (nicotinamide adenine dinucleotide (phosphate))dehydrogenase; mannonate dehydrogenase; mannuronate reductase; mannonate dehydrogenase (NAD(P)+); D-mannonate:nicotinamide adenine dinucleotide (phosphate oxidoreductase (D-mannuronate-forming)) |
Systematic name: |
D-mannonate:NAD(P)+ 6-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-62-7 |
References: |
1. |
Farmer, J.J., III and Eagon, R.G. Aldohexuronic acid catabolism by a soil Aeromonas. J. Bacteriol. 97 (1969) 97–106. [PMID: 4388117] |
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[EC 1.1.1.131 created 1972 (EC 1.2.1.34 created 1972, incorporated 1983; EC 1.1.1.180 created 1983, incorporated 1984)] |
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EC |
1.1.1.132 |
Accepted name: |
GDP-mannose 6-dehydrogenase |
Reaction: |
GDP-D-mannose + 2 NAD+ + H2O = GDP-D-mannuronate + 2 NADH + 2 H+ |
Other name(s): |
guanosine diphosphomannose dehydrogenase; GDP-mannose dehydrogenase; guanosine diphosphomannose dehydrogenase; guanosine diphospho-D-mannose dehydrogenase |
Systematic name: |
GDP-D-mannose:NAD+ 6-oxidoreductase |
Comments: |
Also acts on the corresponding deoxynucleoside diphosphate derivative as a substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-63-8 |
References: |
1. |
Preiss, J. Sugar nucleotide reaction in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate. J. Biol. Chem. 239 (1964) 3127–3132. [PMID: 14245351] |
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[EC 1.1.1.132 created 1972] |
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EC |
1.1.1.133 |
Accepted name: |
dTDP-4-dehydrorhamnose reductase |
Reaction: |
dTDP-β-L-rhamnose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+ |
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For diagram of dtdp-6-deoxyhexose biosynthesis, click here and for diagram of 6-deoxyhexose biosynthesis, click here |
Glossary: |
dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-4-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose |
Other name(s): |
dTDP-4-keto-L-rhamnose reductase; dTDP-4-ketorhamnose reductase; TDP-4-keto-rhamnose reductase; thymidine diphospho-4-ketorhamnose reductase; dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase; dTDP-6-deoxy-β-L-mannose:NADP+ 4-oxidoreductase |
Systematic name: |
dTDP-β-L-rhamnose:NADP+ 4-oxidoreductase |
Comments: |
In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-64-9 |
References: |
1. |
Melo, A. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose. J. Biol. Chem. 243 (1968) 1475–1478. [PMID: 4384782] |
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[EC 1.1.1.133 created 1972] |
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EC |
1.1.1.134 |
Accepted name: |
dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+) |
Reaction: |
dTDP-6-deoxy-β-L-talose + NADP+ = dTDP-4-dehydro-β-L-rhamnose + NADPH + H+ |
Glossary: |
dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
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Other name(s): |
thymidine diphospho-6-deoxy-L-talose dehydrogenase; TDP-6-deoxy-L-talose dehydrogenase; dTDP-6-deoxy-L-talose dehydrogenase (4-reductase); dTDP-6-deoxy-L-talose:NADP+ 4-oxidoreductase |
Systematic name: |
dTDP-6-deoxy-β-L-talose:NADP+ 4-oxidoreductase |
Comments: |
Oxidation on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-65-0 |
References: |
1. |
Gaugler, R.W. and Gabriel, O. Biological mechanisms involved in the formation of deoxy sugars. VII. Biosynthesis of 6-deoxy-L-talose. J. Biol. Chem. 248 (1973) 6041–6049. [PMID: 4199258] |
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[EC 1.1.1.134 created 1972] |
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EC |
1.1.1.135 |
Accepted name: |
GDP-6-deoxy-D-talose 4-dehydrogenase |
Reaction: |
GDP-6-deoxy-α-D-talose + NAD(P)+ = GDP-4-dehydro-α-D-rhamnose + NAD(P)H + H+ |
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For diagram of gdp-l-fucose and GDP-mannose biosynthesis, click here |
Glossary: |
GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
GDP-6-deoxy-α-D-talose = GDP-α-D-pneumose
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Other name(s): |
guanosine diphospho-6-deoxy-D-talose dehydrogenase; GDP-6-deoxy-D-talose:NAD(P)+ 4-oxidoreductase |
Systematic name: |
GDP-6-deoxy-α-D-talose:NAD(P)+ 4-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-66-1 |
References: |
1. |
Markovitz, A. Biosynthesis of guanosine diphosphate D-rhamnose and guanosine diphosphate D-talomethylose from guanosine diphosphate α-D-mannose. J. Biol. Chem. 239 (1964) 2091–2098. [PMID: 14209931] |
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[EC 1.1.1.135 created 1972, modified 1976] |
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EC |
1.1.1.136 |
Accepted name: |
UDP-N-acetylglucosamine 6-dehydrogenase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-α-D-glucuronate + 2 NADH + 2 H+ |
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For diagram of UDP-N-acetylgalactosamine and UDP-N-acetylmannosamine biosynthesis, click here |
Other name(s): |
uridine diphosphoacetylglucosamine dehydrogenase; UDP-acetylglucosamine dehydrogenase; UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase; UDP-GlcNAc dehydrogenase; WbpA; WbpO |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:NAD+ 6-oxidoreductase |
Comments: |
This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-83-5 |
References: |
1. |
Fan, D.-F., John, C.E., Zalitis, J. and Feingold, D.S. UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum. Arch. Biochem. Biophys. 135 (1969) 45–49. [DOI] [PMID: 4312076] |
2. |
Miller, W.L., Wenzel, C.Q., Daniels, C., Larocque, S., Brisson, J.R. and Lam, J.S. Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 279 (2004) 37551–37558. [DOI] [PMID: 15226302] |
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[EC 1.1.1.136 created 1972, modified 2012] |
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EC |
1.1.1.137 |
Accepted name: |
ribitol-5-phosphate 2-dehydrogenase |
Reaction: |
D-ribitol 5-phosphate + NAD(P)+ = D-ribulose 5-phosphate + NAD(P)H + H+ |
Other name(s): |
ribitol 5-phosphate dehydrogenase |
Systematic name: |
D-ribitol-5-phosphate:NAD(P)+ 2-oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD+ and NADP+ as electron acceptor [cf. EC 1.1.1.405, ribitol-5-phosphate 2-dehydrogenase (NADP+)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-67-2 |
References: |
1. |
Glaser, L. Ribitol-5-phosphate dehydrogenase from Lactobacillus plantarum. Biochim. Biophys. Acta 67 (1963) 525–530. [PMID: 13948358] |
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[EC 1.1.1.137 created 1972, modified 2017] |
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EC |
1.1.1.138 |
Accepted name: |
mannitol 2-dehydrogenase (NADP+) |
Reaction: |
D-mannitol + NADP+ = D-fructose + NADPH + H+ |
Other name(s): |
mannitol 2-dehydrogenase (NADP) |
Systematic name: |
D-mannitol:NADP+ 2-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-68-3 |
References: |
1. |
Edmundowicz, J.M. and Wriston, J.C., Jr. Mannitol dehydrogenase from Agaricus campestris. J. Biol. Chem. 238 (1963) 3539–3541. [PMID: 14109183] |
2. |
Strobel, G.A. and Kosuge, T. Polyol metabolism in Diplodia viticola Desm. Arch. Biochem. Biophys. 109 (1965) 622–626. [DOI] [PMID: 14320506] |
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[EC 1.1.1.138 created 1972] |
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EC
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1.1.1.139
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Deleted entry: | polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase |
[EC 1.1.1.139 created 1972, deleted 1978] |
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EC |
1.1.1.140 |
Accepted name: |
sorbitol-6-phosphate 2-dehydrogenase |
Reaction: |
D-sorbitol 6-phosphate + NAD+ = D-fructose 6-phosphate + NADH + H+ |
Other name(s): |
ketosephosphate reductase; ketosephosphate reductase; D-sorbitol 6-phosphate dehydrogenase; D-sorbitol-6-phosphate dehydrogenase; sorbitol-6-P-dehydrogenase; D-glucitol-6-phosphate dehydrogenase |
Systematic name: |
D-sorbitol-6-phosphate:NAD+ 2-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37250-69-4 |
References: |
1. |
Du Toit, P.J. and Kotzé, J.P. The isolation and characterization of sorbitol-6-phosphate dehydrogenase from Clostridium pasteurianum. Biochim. Biophys. Acta 206 (1970) 333–342. [DOI] [PMID: 4318899] |
2. |
Liss, M., Horwitz, S.B. and Kaplan, N.O. D-Mannitol 1-phosphate dehydrogenase and D-sorbitol 6-phosphate dehydrogenase in Aerobacter aerogenes. J. Biol. Chem. 237 (1962) 1342–1350. [PMID: 14465816] |
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[EC 1.1.1.140 created 1972] |
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EC |
1.1.1.141 |
Accepted name: |
15-hydroxyprostaglandin dehydrogenase (NAD+) |
Reaction: |
(5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11α-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+ |
Other name(s): |
NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I); PGDH; 11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase; 15-OH-PGDH; 15-hydroxyprostaglandin dehydrogenase; 15-hydroxyprostanoic dehydrogenase; NAD+-specific 15-hydroxyprostaglandin dehydrogenase; prostaglandin dehydrogenase; 15-hydroxyprostaglandin dehydrogenase (NAD+); (5Z,13E)-(15S)-11α,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase |
Systematic name: |
(5Z,13E,15S)-11α,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase |
Comments: |
Acts on prostaglandin E2, F2α and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-87-9 |
References: |
1. |
Änggaard, E. and Samuelsson, B. Purification and properties of a 15-hydroxyprostaglandin dehydrogenase from swine lung. Prostaglandins 25 (1996) 293–300. |
2. |
Braithwaite, S.S. and Jarabak, J. Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization. J. Biol. Chem. 250 (1975) 2315–2318. [PMID: 1117007] |
3. |
Lee, S.-C. and Levine, L. Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types. J. Biol. Chem. 250 (1975) 548–552. [PMID: 234431] |
4. |
Lee, S.-C., Pong, S.-S., Katzen, D., Wu, K.-Y. and Levine, L. Distribution of prostaglandin E 9-ketoreductase and types I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex. Biochemistry 14 (1975) 142–145. [PMID: 803247] |
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[EC 1.1.1.141 created 1972] |
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EC |
1.1.1.142 |
Accepted name: |
D-pinitol dehydrogenase |
Reaction: |
1D-3-O-methyl-chiro-inositol + NADP+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADPH + H+ |
Other name(s): |
5D-5-O-methyl-chiro-inositol:NADP+ oxidoreductase |
Systematic name: |
1D-3-O-methyl-chiro-inositol:NADP+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-71-8 |
References: |
1. |
Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442–448. [DOI] [PMID: 4389340] |
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[EC 1.1.1.142 created 1972] |
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EC |
1.1.1.143 |
Accepted name: |
sequoyitol dehydrogenase |
Reaction: |
5-O-methyl-myo-inositol + NAD+ = 2D-5-O-methyl-2,3,5/4,6-pentahydroxycyclohexanone + NADH + H+ |
Other name(s): |
D-pinitol dehydrogenase |
Systematic name: |
5-O-methyl-myo-inositol:NAD+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-72-9 |
References: |
1. |
Ruis, H. and Hoffmann-Ostenhof, O. Enzymic epimerization of sequoyitol to D-pinitol in Trifolium incarnatum. Eur. J. Biochem. 7 (1969) 442–448. [DOI] [PMID: 4389340] |
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[EC 1.1.1.143 created 1972] |
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EC |
1.1.1.144 |
Accepted name: |
perillyl-alcohol dehydrogenase |
Reaction: |
perillyl alcohol + NAD+ = perillyl aldehyde + NADH + H+ |
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For diagram of (-)-carvone, perillyl aldehyde and pulegone biosynthesis, click here |
Other name(s): |
perillyl alcohol dehydrogenase |
Systematic name: |
perillyl-alcohol:NAD+ oxidoreductase |
Comments: |
Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-73-0 |
References: |
1. |
Ballal, N.R., Bhattacharyya, P.K. and Rangachari, P.N. Perillyl alcohol dehydrogenase from a soil pseudomonad. Biochem. Biophys. Res. Commun. 23 (1966) 473–478. [DOI] [PMID: 4289759] |
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[EC 1.1.1.144 created 1972] |
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EC |
1.1.1.145 |
Accepted name: |
3β-hydroxy-Δ5-steroid dehydrogenase |
Reaction: |
a 3β-hydroxy-Δ5-steroid + NAD+ = a 3-oxo-Δ5-steroid + NADH + H+ |
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For diagram of cholesterol catabolism (rings a, B and c), click here |
Other name(s): |
progesterone reductase; Δ5-3β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene steroid dehydrogenase; 3β-hydroxy steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid oxidoreductase; 3β-hydroxy-5-ene-steroid oxidoreductase; steroid-Δ5-3β-ol dehydrogenase; 3β-HSDH; 5-ene-3-β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene-steroid dehydrogenase |
Systematic name: |
3β-hydroxy-Δ5-steroid:NAD+ 3-oxidoreductase |
Comments: |
This activity is found in several bifunctional enzymes that catalyse the oxidative conversion of Δ5-3-hydroxy steroids to a Δ4-3-oxo configuration. This conversion is carried out in two separate, sequential reactions; in the first reaction, which requires NAD+, the enzyme catalyses the dehydrogenation of the 3β-hydroxy steroid to a 3-oxo intermediate. In the second reaction the reduced cosubstrate, which remains attached to the enzyme, activates the isomerization of the Δ5 form to a Δ4 form (cf. EC 5.3.3.1, steroid Δ-isomerase). Substrates include dehydroepiandrosterone (which is converted into androst-5-ene-3,17-dione), pregnenolone (converted to progesterone) and cholest-5-en-3-one, an intermediate of cholesterol degradation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-85-3 |
References: |
1. |
Cheatum, S.G. and Warren, J.C. Purification and properties of 3-β-hydroxysteroid dehydrogenase and Δ-5-3-ketosteroid isomerase from bovine corpora lutea. Biochim. Biophys. Acta 122 (1966) 1–13. [PMID: 4226148] |
2. |
Koritz, S.B. The conversion of prepnenolone to progesterone by small particle from rat adrenal. Biochemistry 3 (1964) 1098–1102. [PMID: 14220672] |
3. |
Neville, A.M., Orr, J.C. and Engel, L.L. Δ5-3β-Hydroxy steroid dehydrogenase activities of bovine adrenal cortex. Biochem. J. 107 (1968) 20. |
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[EC 1.1.1.145 created 1972] |
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EC |
1.1.1.146 |
Accepted name: |
11β-hydroxysteroid dehydrogenase |
Reaction: |
an 11β-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH + H+ |
Other name(s): |
corticosteroid 11β-dehydrogenase; β-hydroxysteroid dehydrogenase; 11β-hydroxy steroid dehydrogenase; corticosteroid 11-reductase; dehydrogenase, 11β-hydroxy steroid |
Systematic name: |
11β-hydroxysteroid:NADP+ 11-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9041-46-7 |
References: |
1. |
Agarwal, A.K., Monder, C., Eckstein, B. and White, P.C. Cloning and expression of rat cDNA encoding corticosteroid 11β-dehydrogenase. J. Biol. Chem. 264 (1989) 18939–18943. [PMID: 2808402] |
2. |
Bush, I.E., Hunter, S.A. and Meigs, R.A. Metabolism of 11-oxygenated steroids. Metabolism in vitro by preparations of liver. Biochem. J. 107 (1968) 239–258. [PMID: 4384445] |
3. |
Lakshmi, V. and Monder, C. Purification and characterization of the corticosteroid 11β-dehydrogenase component of the rat liver 11β-hydroxysteroid dehydrogenase complex. Endocrinology 123 (1988) 2390–2398. [DOI] [PMID: 3139396] |
4. |
Phillips, D.M., Lakshmi, V. and Monder, C. Corticosteroid 11β-dehydrogenase in rat testis. Endocrinology 125 (1989) 209–216. [DOI] [PMID: 2661206] |
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[EC 1.1.1.146 created 1972] |
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EC |
1.1.1.147 |
Accepted name: |
16α-hydroxysteroid dehydrogenase |
Reaction: |
a 16α-hydroxysteroid + NAD(P)+ = a 16-oxosteroid + NAD(P)H + H+ |
Other name(s): |
16α-hydroxy steroid dehydrogenase |
Systematic name: |
16α-hydroxysteroid:NAD(P)+ 16-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-74-1 |
References: |
1. |
Meigs, R.A. and Ryan, K.J. 16-α-Hydroxysteroid dehydrogenase of rat kidney. Purification, assay, and properties. J. Biol. Chem. 241 (1966) 4011–4015. [PMID: 4380686] |
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[EC 1.1.1.147 created 1972] |
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EC |
1.1.1.148 |
Accepted name: |
estradiol 17α-dehydrogenase |
Reaction: |
estradiol-17α + NAD(P)+ = estrone + NAD(P)H + H+ |
Other name(s): |
17α-estradiol dehydrogenase; 17α-hydroxy steroid dehydrogenase; 17α-hydroxy steroid oxidoreductase; 17α-hydroxysteroid oxidoreductase; estradiol 17α-oxidoreductase |
Systematic name: |
17α-hydroxysteroid:NAD(P)+ 17-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9044-91-1 |
References: |
1. |
Renwick, A.G.C. and Engel, L.L. The partial purification of 17α- and 17β-estradiol dehydrogenase activities from chicken liver. Biochim. Biophys. Acta 146 (1967) 336–348. [DOI] [PMID: 4383682] |
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[EC 1.1.1.148 created 1972] |
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EC |
1.1.1.149 |
Accepted name: |
20α-hydroxysteroid dehydrogenase |
Reaction: |
17α,20α-dihydroxypregn-4-en-3-one + NAD(P)+ = 17α-hydroxyprogesterone + NAD(P)H + H+ |
Other name(s): |
20α-hydroxy steroid dehydrogenase; 20α-HSD; 20α-HSDH |
Systematic name: |
20α-hydroxysteroid:NAD(P)+ 20-oxidoreductase |
Comments: |
Re-specific with respect to NAD(P)+ (cf. EC 1.1.1.62 17β-estradiol 17-dehydrogenase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9040-08-8 |
References: |
1. |
Shikita, M., Inano, H. and Tamaoki, B. Further studies on 20α-hydroxysteroid dehydrogenase of rat testes. Biochemistry 6 (1967) 1760–1764. [PMID: 4382486] |
2. |
Strickler, R.C., Tobias, B. and Covey, D.F. Human placental 17β-estradiol dehydrogenase and 20α-hydroxysteroid dehydrogenase. Two activities at a single enzyme active site. J. Biol. Chem. 256 (1981) 316–321. [PMID: 6935192] |
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[EC 1.1.1.149 created 1972, deleted 1983, reinstated 1986] |
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EC |
1.1.1.150 |
Accepted name: |
21-hydroxysteroid dehydrogenase (NAD+) |
Reaction: |
pregnan-21-ol + NAD+ = pregnan-21-al + NADH + H+ |
Other name(s): |
21-hydroxysteroid dehydrogenase (NAD) |
Systematic name: |
21-hydroxysteroid:NAD+ 21-oxidoreductase |
Comments: |
Acts on a number of 21-hydroxycorticosteroids. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-75-2 |
References: |
1. |
Monder, C. and White, A. The 21-hydroxysteroid dehydrogenases of liver. A nicotinamide adenine dinucleotide phosphate dehydrogenase and two nicotinamide adenine dinucleotide dehydrogenases. J. Biol. Chem. 240 (1965) 71–77. [PMID: 14253469] |
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[EC 1.1.1.150 created 1972] |
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