EC |
1.14.13.232 |
Accepted name: |
6-methylpretetramide 4-monooxygenase |
Reaction: |
6-methylpretetramide + NADPH + H+ + O2 = 4-hydroxy-6-methylpretetramide + NADP+ + H2O |
Glossary: |
6-methylpretetramide = 1,3,10,11,12-pentahydroxy-6-methyltetracene-2-carboxamide
4-hydroxy-6-methylpretetramide = 1,3,4,10,11,12-hexahydroxy-6-methyltetracene-2-carboxamide |
Systematic name: |
6-methylpretetramide,NADPH:oxygen oxidoreductase (4-hydroxylating) |
Comments: |
The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. That bacterium possesses two enzymes that can catalyse the reaction - OxyE is the main isozyme, while OxyL has a lower activity. OxyL is bifunctional, and its main function is EC 1.14.13.233, 4-hydroxy-6-methylpretetramide 12a-monooxygenase. Contains FAD. |
References: |
1. |
Zhang, W., Watanabe, K., Cai, X., Jung, M.E., Tang, Y. and Zhan, J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068–6069. [PMID: 18422316] |
2. |
Wang, P., Zhang, W., Zhan, J. and Tang, Y. Identification of OxyE as an ancillary oxygenase during tetracycline biosynthesis. ChemBioChem 10 (2009) 1544–1550. [PMID: 19472250] |
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[EC 1.14.13.232 created 2016] |
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EC |
1.14.13.233 |
Accepted name: |
4-hydroxy-6-methylpretetramide 12a-monooxygenase |
Reaction: |
4-hydroxy-6-methylpretetramide + NADPH + H+ + O2 = 4-de(dimethylamino)-4-oxoanhydrotetracycline + NADP+ + H2O |
Glossary: |
4-hydroxy-6-methylpretetramide = 1,3,4,10,11,12-hexahydroxy-6-methyltetracene-2-carboxamide
4-de(dimethylamino)-4-oxoanhydrotetracycline = (4aR,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-1,4,12-trioxo-4a,5-dihydrotetracene-2-carboxamide |
Other name(s): |
oxyL (gene name) |
Systematic name: |
4-hydroxy-6-methylpretetramide,NADPH:oxygen oxidoreductase (12a-hydroxylating) |
Comments: |
Contains FAD. The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. The enzyme is bifunctional, and can also catalyse EC 1.14.13.232, 6-methylpretetramide 4-monooxygenase. |
References: |
1. |
Zhang, W., Watanabe, K., Cai, X., Jung, M.E., Tang, Y. and Zhan, J. Identifying the minimal enzymes required for anhydrotetracycline biosynthesis. J. Am. Chem. Soc. 130 (2008) 6068–6069. [PMID: 18422316] |
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[EC 1.14.13.233 created 2016] |
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