| EC |
1.14.14.15 |
| Accepted name: |
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] monooxygenase |
| Reaction: |
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = (3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FAD + H2O |
| Other name(s): |
SgcC |
| Systematic name: |
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2],FADH2:oxygen oxidoreductase (5-hydroxylating) |
| Comments: |
The enzyme from the bacterium Streptomyces globisporus is involved in the biosynthesis of the (S)-3-chloro-5-hydroxy-β-tyrosine moiety prior to incorporation into the chromoprotein antitumor antibiotic C-1027. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Lin, S., Van Lanen, S.G. and Shen, B. Characterization of the two-component, FAD-dependent monooxygenase SgcC that requires carrier protein-tethered substrates for the biosynthesis of the enediyne antitumor antibiotic C-1027. J. Am. Chem. Soc. 130 (2008) 6616–6623. [DOI] [PMID: 18426211] |
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| [EC 1.14.14.15 created 2014] |
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