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Literature summary for 1.14.13.232 extracted from

  • Wang, P.; Zhang, W.; Zhan, J.; Tang, Y.
    Identification of oxyE as an ancillary oxygenase during tetracycline biosynthesis (2009), ChemBioChem, 10, 1544-1550.
    View publication on PubMed
Search for more literature for 1.14.13.232

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 Q3S8R0
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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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Streptomyces rimosus ATCC 10970 Q3S8R0
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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
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 ?
6-methylpretetramide + NADPH + H+ + O2
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 Streptomyces rimosus ATCC 10970 4-hydroxy-6-methylpretetramide + NADP+ + H2O
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 ?

Synonyms

Synonyms Comment Organism
OxyE
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 Streptomyces rimosus
oxyL
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 Streptomyces rimosus

Cofactor

Cofactor Comment Organism Structure
FAD
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 Streptomyces rimosus

General Information

General Information Comment Organism
physiological function a gene disruption mutant reveals the complete disappearance of oxytetracycline, with the concomitant appearance of a predominant glycoside metabolite derived from 4-hydroxy-6-methylpretetramid Streptomyces rimosus
physiological function OxyE plays a nonessential, but important role in oxytetracycline biosynthesis by serving as a efficient C-4 hydroxylase. A gene disruption mutant produces only about 50% of the oxytetracycline found in wild-type, and additionally synthesizes a glycoside derivative of 6-methylpretetramide Streptomyces rimosus