EC |
1.11.1.7 |
Accepted name: |
peroxidase |
Reaction: |
2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O |
Other name(s): |
lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase |
Systematic name: |
phenolic donor:hydrogen-peroxide oxidoreductase |
Comments: |
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3′,5,5′-tetramethylbenzidine (TMB) and 2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9003-99-0 |
References: |
1. |
Kenten, R.H. and Mann, P.J.G. Simple method for the preparation of horseradish peroxidase. Biochem. J. 57 (1954) 347–348. [PMID: 13172193] |
2. |
Morrison, M., Hamilton, H.B. and Stotz, E. The isolation and purification of lactoperoxidase by ion exchange chromatography. J. Biol. Chem. 228 (1957) 767–776. [PMID: 13475358] |
3. |
Paul, K.G. Peroxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 227–274. |
4. |
Tagawa, K., Shin, M. and Okunuki, K. Peroxidases from wheat germ. Nature (Lond.) 183 (1959) 111. [PMID: 13622706] |
5. |
Theorell, H. The preparation and some properties of crystalline horse-radish peroxidase. Ark. Kemi Mineral. Geol. 16A No. 2 (1943) 1–11. |
6. |
Farhangrazi, Z.S., Copeland, B.R., Nakayama, T., Amachi, T., Yamazaki, I. and Powers, L.S. Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase. Biochemistry 33 (1994) 5647–5652. [PMID: 8180190] |
7. |
Aitken, M.D. and Heck, P.E. Turnover capacity of coprinus cinereus peroxidase for phenol and monosubstituted phenol. Biotechnol. Prog. 14 (1998) 487–492. [DOI] [PMID: 9622531] |
8. |
Dunford, H.B. Heme peroxidases, Wiley-VCH, New York, 1999, pp. 33–218. |
9. |
Torres, E and Ayala, M. Biocatalysis based on heme peroxidases, Springer, Berlin, 2010, pp. 7–110. |
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[EC 1.11.1.7 created 1961, modified 2011] |
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EC |
1.14.11.60 |
Accepted name: |
scopoletin 8-hydroxylase |
Reaction: |
scopoletin + 2-oxoglutarate + O2 = fraxetin + succinate + CO2 |
Glossary: |
fraxetin = 7,8-dihydroxy-6-methoxy-2H-chromen-2-one
scopoletin = 7-hydroxy-6-methoxy-2H-chromen-2-one |
Other name(s): |
S8H (gene name) |
Systematic name: |
scopoletin,2-oxoglutarate:oxygen oxidoreductase (8-hydroxylating) |
Comments: |
Requires iron(II) and ascorbate. A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Siwinska, J., Siatkowska, K., Olry, A., Grosjean, J., Hehn, A., Bourgaud, F., Meharg, A.A., Carey, M., Lojkowska, E. and Ihnatowicz, A. Scopoletin 8-hydroxylase: a novel enzyme involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis. J. Exp. Bot. 69 (2018) 1735–1748. [PMID: 29361149] |
2. |
Rajniak, J., Giehl, R.FH., Chang, E., Murgia, I., von Wiren, N. and Sattely, E.S. Biosynthesis of redox-active metabolites in response to iron deficiency in plants. Nat. Chem. Biol. 14 (2018) 442–450. [PMID: 29581584] |
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[EC 1.14.11.60 created 2018] |
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EC |
1.14.11.61 |
Accepted name: |
feruloyl-CoA 6-hydroxylase |
Reaction: |
trans-feruloyl-CoA + 2-oxoglutarate + O2 = trans-6-hydroxyferuloyl-CoA + succinate + CO2 |
Glossary: |
trans-feruloyl-CoA = 4-hydroxy-3-methoxycinnamoyl-CoA = (E)-3-(4-hydroxy-3-methoxyphenyl)propenoyl-CoA |
Systematic name: |
feruloyl-CoA,2-oxoglutarate:oxygen oxidoreductase (6-hydroxylating) |
Comments: |
Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA. cf. EC 1.14.11.62, trans-4-coumaroyl-CoA 2-hydroxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kai, K., Mizutani, M., Kawamura, N., Yamamoto, R., Tamai, M., Yamaguchi, H., Sakata, K. and Shimizu, B. Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana. Plant J. 55 (2008) 989–999. [PMID: 18547395] |
2. |
Bayoumi, S.A., Rowan, M.G., Blagbrough, I.S. and Beeching, J.R. Biosynthesis of scopoletin and scopolin in cassava roots during post-harvest physiological deterioration: the E-Z-isomerisation stage. Phytochemistry 69 (2008) 2928–2936. [PMID: 19004461] |
3. |
Vialart, G., Hehn, A., Olry, A., Ito, K., Krieger, C., Larbat, R., Paris, C., Shimizu, B., Sugimoto, Y., Mizutani, M. and Bourgaud, F. A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-coumaroyl CoA 2′-hydroxylase activity (C2′H): a missing step in the synthesis of umbelliferone in plants. Plant J. 70 (2012) 460–470. [DOI] [PMID: 22168819] |
4. |
Matsumoto, S., Mizutani, M., Sakata, K. and Shimizu, B. Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam. Phytochemistry 74 (2012) 49–57. [PMID: 22169019] |
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[EC 1.14.11.61 created 2019] |
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EC |
1.14.11.62 |
Accepted name: |
trans-4-coumaroyl-CoA 2-hydroxylase |
Reaction: |
trans-4-coumaroyl-CoA + 2-oxoglutarate + O2 = 2,4-dihydroxycinnamoyl-CoA + succinate + CO2 |
Glossary: |
trans-4-coumaroyl-CoA = (2E)-3-(4-hydroxyphenyl)prop-2-enoyl-CoA
2,4-dihydroxycinnamoyl-CoA = (2E)-3-(2,4-dihydroxyphenyl)prop-2-enoyl-CoA
umbelliferone = 7-hydroxycoumarin |
Other name(s): |
Diox4 (gene name); C2′H (gene name) |
Systematic name: |
(2E)-3-(4-hydroxyphenyl)prop-2-enoyl-CoA,2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating) |
Comments: |
Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization followed by lactonization and cyclization, liberating CoA and forming umbelliferone. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-feruloyl-CoA (cf. EC 1.14.11.61, feruloyl-CoA 6-hydroxylase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Vialart, G., Hehn, A., Olry, A., Ito, K., Krieger, C., Larbat, R., Paris, C., Shimizu, B., Sugimoto, Y., Mizutani, M. and Bourgaud, F. A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-coumaroyl CoA 2′-hydroxylase activity (C2′H): a missing step in the synthesis of umbelliferone in plants. Plant J. 70 (2012) 460–470. [DOI] [PMID: 22168819] |
2. |
Matsumoto, S., Mizutani, M., Sakata, K. and Shimizu, B. Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam. Phytochemistry 74 (2012) 49–57. [PMID: 22169019] |
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[EC 1.14.11.62 created 2019] |
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EC |
2.4.1.104 |
Accepted name: |
o-dihydroxycoumarin 7-O-glucosyltransferase |
Reaction: |
UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin |
Other name(s): |
uridine diphosphoglucose-o-dihydroxycoumarin 7-O-glucosyltransferase; UDP-glucose:o-dihydroxycoumarin glucosyltransferase |
Systematic name: |
UDP-glucose:7,8-dihydroxycoumarin 7-O-β-D-glucosyltransferase |
Comments: |
Converts the aglycone daphetin into daphnin and, more slowly, esculetin into cichoriin, umbelliferone into skimmin, hydrangetin into hydrangin and scopoletin into scopolin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74114-37-7 |
References: |
1. |
Ibrahim, R.K. and Boulay, B. Purification and some properties of UDP-glucose:o-hydroxycoumarin 7-O-glucosyltransferase from tobacco cell cultures. Plant Sci. Lett. 18 (1980) 177–184. |
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[EC 2.4.1.104 created 1983] |
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EC |
2.4.1.128 |
Accepted name: |
scopoletin glucosyltransferase |
Reaction: |
UDP-glucose + scopoletin = UDP + scopolin |
Other name(s): |
uridine diphosphoglucose-scopoletin glucosyltransferase; UDP-glucose:scopoletin glucosyltransferase; SGTase |
Systematic name: |
UDP-glucose:scopoletin O-β-D-glucosyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81210-69-7 |
References: |
1. |
Hino, F., Okazaki, M. and Miura, Y. Effect of 2,4-dichlorophenoxyacetic acid on glucosylation of scopoletin to scopolin in tobacco tissue-culture. Plant Physiol. 69 (1982) 810–813. [PMID: 16662301] |
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[EC 2.4.1.128 created 1984] |
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