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Literature summary for 1.14.13.232 extracted from

  • Zhang, W.; Watanabe, K.; Cai, X.; Jung, M.; Tang, Y.; Zhan, J.
    Identifying the minimal enzymes required for anhydrotetracycline biosynthesis (2008), J. Am. Chem. Soc., 130, 6068-6069.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptomyces rimosus

Organism

Organism UniProt Comment Textmining
Streptomyces rimosus Q3S8Q4 bifunctional enzyme, hydroxylates 6-methylpretetramide at both the C-12a and C-4 positions, i.e. reactions of EC 1.14.13.232 and EC 1.14.1.3.233
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Streptomyces rimosus ATCC 10970 Q3S8Q4 bifunctional enzyme, hydroxylates 6-methylpretetramide at both the C-12a and C-4 positions, i.e. reactions of EC 1.14.13.232 and EC 1.14.1.3.233
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-methylpretetramide + NADPH + H+ + O2
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Streptomyces rimosus 4-hydroxy-6-methylpretetramide + NADP+ + H2O
-
?
6-methylpretetramide + NADPH + H+ + O2
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Streptomyces rimosus ATCC 10970 4-hydroxy-6-methylpretetramide + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
oxyL
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Streptomyces rimosus

Cofactor

Cofactor Comment Organism Structure
NADPH
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Streptomyces rimosus

General Information

General Information Comment Organism
physiological function OxyL is a NADPH-dependent dioxygenase that hydroxylates 6-methylpretetramide at both C12a and C4 positions Streptomyces rimosus