EC |
1.1.1.340 |
Accepted name: |
1-deoxy-11β-hydroxypentalenate dehydrogenase |
Reaction: |
1-deoxy-11β-hydroxypentalenate + NAD+ = 1-deoxy-11-oxopentalenate + NADH + H+ |
Glossary: |
1-deoxy-11β-hydroxypentalenate = (1S,2R,3aR,5aS,8aR)-2-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate |
Other name(s): |
1-deoxy-11β-hydroxypentalenic acid dehydrogenase; ptlF (gene name); penF (gene name) |
Systematic name: |
1-deoxy-11β-hydroxypentalenate:NAD+ oxidoreductase |
Comments: |
Isolated from the bacterium Streptomyces avermitilis and present in many other Streptomyces species. Part of the pathway for pentalenolactone biosynthesis. |
References: |
1. |
You, Z., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis: Molecular cloning and assignment of biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces avermitilis, and identification of a new biosynthetic intermediate. Arch. Biochem. Biophys. 459 (2007) 233–240. [PMID: 17178094] |
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[EC 1.1.1.340 created 2012] |
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EC
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1.3.7.10
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Transferred entry: | pentalenolactone synthase. Now EC 1.14.19.8, pentalenolactone synthase
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[EC 1.3.7.10 created 2012, deleted 2013] |
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EC |
1.14.11.35 |
Accepted name: |
1-deoxypentalenic acid 11β-hydroxylase |
Reaction: |
1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11β-hydroxypentalenate + succinate + CO2 |
Glossary: |
1-deoxypentalenate = (1R,3aR,5aS,8aR)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
1-deoxy-11β-hydroxypentalenate = (1S,2R,3aR,5aS,8aR)-2-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate |
Other name(s): |
ptlH (gene name); sav2991 (gene name); pntH (gene name) |
Systematic name: |
1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase |
Comments: |
The enzyme requires iron(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis. |
References: |
1. |
You, Z., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis. J. Am. Chem. Soc. 128 (2006) 6566–6567. [PMID: 16704250] |
2. |
You, Z., Omura, S., Ikeda, H., Cane, D.E. and Jogl, G. Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis. J. Biol. Chem. 282 (2007) 36552–36560. [PMID: 17942405] |
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[EC 1.14.11.35 created 2012] |
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EC |
1.14.11.36 |
Accepted name: |
pentalenolactone F synthase |
Reaction: |
pentalenolactone D + 2 2-oxoglutarate + 2 O2 = pentalenolactone F + 2 succinate + 2 CO2 + H2O (overall reaction) (1a) pentalenolactone D + 2-oxoglutarate + O2 = pentalenolactone E + succinate + CO2 + H2O (1b) pentalenolactone E + 2-oxoglutarate + O2 = pentalenolactone F + succinate + CO2 |
Glossary: |
pentalenolactone D = (1S,4aR,6aS,9aR)-1,8,8-trimethyl-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate
pentalenolactone E = (4aR,6aS,9aR)-8,8-dimethyl-1-methylene-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate
pentalenolactone F = (1′R,4′aR,6′aS,9′aR)-8′,8′-dimethyl-2′-oxo-4′,4′a,6′a,8′,9′-hexahydrospiro[oxirane-2,1′-pentaleno[1,6a-c]pyran]-5′-carboxylic acid |
Other name(s): |
penD (gene name); pntD (gene name); ptlD (gene name) |
Systematic name: |
pentalenolactone-D,2-oxoglutarate:oxygen oxidoreductase |
Comments: |
Requires iron(II) and ascorbate. Isolated from the bacteria Streptomyces exfoliatus, Streptomyces arenae and Streptomyces avermitilis. Part of the pentalenolactone biosynthesis pathway. |
References: |
1. |
Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739–1754. [PMID: 21250661] |
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[EC 1.14.11.36 created 2012] |
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EC
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1.14.13.133
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Transferred entry: | pentalenene oxygenase. Now EC 1.14.15.32, pentalenene oxygenase
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[EC 1.14.13.133 created 2011, deleted 2018] |
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EC |
1.14.13.170 |
Accepted name: |
pentalenolactone D synthase |
Reaction: |
1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = pentalenolactone D + NADP+ + H2O |
Glossary: |
1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
pentalenolactone D = (1S,4aR,6aS,9aR)-1,8,8-trimethyl-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate |
Other name(s): |
penE (gene name); pntE (gene name) |
Systematic name: |
1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (pentalenolactone-D-forming) |
Comments: |
A FAD-dependent oxygenase. Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae. The ketone undergoes a biological Baeyer-Villiger reaction. Part of the pathway of pentalenolactone biosynthesis. |
References: |
1. |
Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739–1754. [PMID: 21250661] |
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[EC 1.14.13.170 created 2012] |
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EC |
1.14.13.171 |
Accepted name: |
neopentalenolactone D synthase |
Reaction: |
1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = neopentalenolactone D + NADP+ + H2O |
Glossary: |
1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
neopentalenolactone D = (1S,4aR,6aS)-1,7,7-trimethyl-3-oxo-4,4a,6a,7,8,9-hexahydro-3H-pentaleno[6a,1-c]pyran-5-carboxylate |
Other name(s): |
ptlE (gene name) |
Systematic name: |
1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (neopentalenolactone-D-forming) |
Comments: |
A FAD-dependent oxygenase. Isolated from the bacterium Streptomyces avermitilis. The ketone undergoes a biological Baeyer-Villiger reaction. |
References: |
1. |
Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739–1754. [PMID: 21250661] |
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[EC 1.14.13.171 created 2012] |
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EC |
1.14.15.11 |
Accepted name: |
pentalenic acid synthase |
Reaction: |
1-deoxypentalenate + reduced ferredoxin + O2 = pentalenate + oxidized ferredoxin + H2O |
Glossary: |
1-deoxypentalenate = (1R,3aR,5aS,8aR)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
pentalenate = (1R,3aR,5aS,6R,8aS)-6-hydroxy-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate |
Other name(s): |
CYP105D7; sav7469 (gene name); 1-deoxypentalenate,reduced ferredoxin:O2 oxidoreductase |
Systematic name: |
1-deoxypentalenate,reduced ferredoxin:oxygen oxidoreductase |
Comments: |
A heme-thiolate enzyme (P-450). Isolated from the bacterium Streptomyces avermitilis. The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis. |
References: |
1. |
Takamatsu, S., Xu, L.H., Fushinobu, S., Shoun, H., Komatsu, M., Cane, D.E. and Ikeda, H. Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis. J. Antibiot. (Tokyo) 64 (2011) 65–71. [PMID: 21081950] |
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[EC 1.14.15.11 created 2012] |
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EC |
1.14.15.32 |
Accepted name: |
pentalenene oxygenase |
Reaction: |
pentalenene + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = pentalen-13-al + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction) (1a) pentalenene + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-ol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O (1b) pentalen-13-ol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-al + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
Other name(s): |
PtlI |
Systematic name: |
pentalenene,reduced ferredoxin:oxygen 13-oxidoreductase |
Comments: |
A cytochrome P-450 (heme-thiolate) protein found in the bacterium Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics. |
References: |
1. |
Quaderer, R., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis. J. Am. Chem. Soc. 128 (2006) 13036–13037. [PMID: 17017767] |
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[EC 1.14.15.32 created 2011 as EC 1.14.13.133, transferred 2018 to EC 1.14.15.32] |
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EC |
1.14.19.8 |
Accepted name: |
pentalenolactone synthase |
Reaction: |
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+ = pentalenolactone + 2 oxidized ferredoxin + 2 H2O |
Glossary: |
pentalenolactone F = (1R,4aR,6aS,9aR)-8,8-dimethyl-2-oxo-4,4a,6a,8,9-hexahydrospiro[oxirane-2,1-pentaleno[1,6a-c]pyran]-5-carboxylic acid
pentalenolactone = (1R,4aR,6aR,7S,9aS)-7,8-dimethyl-2-oxo-4,4a,6a,7-tetrahydrospiro[oxirane-2,1-pentaleno[1,6a-c]pyran]-5-carboxylic acid
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Other name(s): |
penM (gene name); pntM (gene name) |
Systematic name: |
pentalenolactone-reduced-ferredoxin:oxygen oxidoreductase (pentalenolactone-forming) |
Comments: |
A heme-thiolate protein (P-450). Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae. |
References: |
1. |
Zhu, D., Seo, M.J., Ikeda, H. and Cane, D.E. Genome mining in streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone. J. Am. Chem. Soc. 133 (2011) 2128–2131. [PMID: 21284395] |
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[EC 1.14.19.8 created 2012 as EC 1.3.7.10, transferred 2013 to EC 1.14.19.8] |
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EC |
4.2.3.7 |
Accepted name: |
pentalenene synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate = pentalenene + diphosphate |
Glossary: |
pentalenene = (1R,8aR)-1,4,7,7-tetramethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene |
Other name(s): |
pentalenene synthetase |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, pentalenene-forming) |
Comments: |
Isolated from Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics. The 9si hydrogen of farnesyl diphosphate undergoes a 1,2-hydride shift where it becomes the 1α hydrogen of pentalenene. |
References: |
1. |
Cane, D.E. Cell-free studies of monoterpene and sesquiterpene biosynthesis. Biochem. Soc. Trans. 11 (1983) 510–515. [PMID: 6642060] |
2. |
Cane, D.E. and Tillman, A.M. Pentalenene biosynthesis and the enzymic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc. 105 (1983) 122–124. |
3. |
Cane, D.E., Sohng, J.K., Lamberson, C.R., Rudnicki, S.M., Wu, Z., Lloyd, M.D., Oliver, J.S. and Hubbard, B.R. Pentalenene synthase. Purification, molecular cloning, sequencing, and
high-level expression in Escherichia coli of a terpenoid cyclase from
Streptomyces UC5319. Biochemistry 33 (1994) 5846–5857. [PMID: 8180213] |
4. |
Cane, D.E., Abell, C., Harrison, P.H., Hubbard, B.R., Kane, C.T., Lattman, R., Oliver, J.S. and Weiner, S.W. Terpenoid biosynthesis and the stereochemistry of enzyme-catalysed allylic addition-elimination reactions. Philos. Trans. R. Soc. Lond. B Biol. Sci. 332 (1991) 123–129. [PMID: 1678531] |
5. |
Lesburg, C.A., Zhai, G., Cane, D.E. and Christianson, D.W. Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology. Science 277 (1997) 1820–1824. [PMID: 9295272] |
6. |
Zu, L., Xu, M., Lodewyk, M.W., Cane, D.E., Peters, R.J. and Tantillo, D.J. Effect of isotopically sensitive branching on product distribution for pentalenene synthase: support for a mechanism predicted by quantum chemistry. J. Am. Chem. Soc. 134 (2012) 11369–11371. [PMID: 22738258] |
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[EC 4.2.3.7 created 1989 as EC 4.6.1.5, transferred 2000 to EC 4.2.3.7] |
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