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Reference on EC 1.14.14.15 - (3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] monooxygenase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lin, S.; van Lanen, S.G., Shen, B.
Regiospecific chlorination of (S)-beta-tyrosyl-S-carrier protein catalyzed by SgcC3 in the biosynthesis of the enediyne antitumor antibiotic C-1027
J. Am. Chem. Soc.
129
12432-12438
2007
Streptomyces globisporus
Manually annotated by BRENDA team
Lin, S.; Van Lanen, S.G.; 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
6616-6623
2008
Streptomyces globisporus
Manually annotated by BRENDA team
Van Lanen, S.G.; Dorrestein, P.C.; Christenson, S.D.; Liu, W.; Ju, J.; Kelleher, N.L.; Shen, B.
Biosynthesis of the beta-amino acid moiety of the enediyne antitumor antibiotic C-1027 featuring beta-amino acyl-S-carrier protein intermediates
J. Am. Chem. Soc.
127
11594-11595
2005
Streptomyces globisporus
Manually annotated by BRENDA team
Chang, C.; Lohman, J.; Cao, H.; Tan, K.; Rudolf, J.; Ma, M.; Xu, W.; Bingman, C.; Yennamalli, R.; Bigelow, L.; Babnigg, G.; Yan, X.; Joachimiak, A.; Phillips, G.; Shen, B.
Crystal structures of SgcE6 and SgcC, the two-component monooxygenase that catalyzes hydroxylation of a carrier protein-tethered substrate during the biosynthesis of the enediyne antitumor antibiotic C-1027 in Streptomyces globisporus
Biochemistry
55
5142-5154
2016
Streptomyces globisporus (Q8GME2 and Q8GMG6)
Manually annotated by BRENDA team