(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] monooxygenase;
SgcC
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2],FADH2:oxygen oxidoreductase (5-hydroxylating)
Reaction(IUBMB)
(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
(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2];
FADH2 [CPD:C01352];
O2 [CPD:C00007]
Product
(3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2];
FAD [CPD:C00016];
H2O [CPD:C00001]
Comment
The enzyme from the bacterium Streptomyces globisporus is involved in the biosynthesis of the (S)-3-chloro-5-hydroxy-beta-tyrosine moiety prior to incorporation into the chromoprotein antitumor antibiotic C-1027.
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.
