Studies on the biosynthesis of bialaphos (SF-1293) 12. C-P bond formation mechanism of bialaphos: discovery of a P-methylation enzyme.
An enzymatic activity catalyzing P-methylation of N-acetyldemethylphosphinothricin, a biosynthetic intermediate of the herbicide bialaphos, was detected in a cell extract of Streptomyces hygroscopicus SF-1293, a bialaphos producing organism. The gene coding for this P-methylation enzyme in the bialaphos biosynthetic gene cluster was also expressed in Streptomyces lividans. The methyl donor of the reaction was determined to be methylcobalamin. The P-methylation enzyme utilized both N-acetyldemethylbialaphos and N-acetyldemethylphosphinothricin as substrates.
Kamigiri
K
K
Institute of Applied Microbiology, University of Tokyo, Japan.
Hidaka
T
T
Imai
S
S
Murakami
T
T
Seto
H
H
D006540:Herbicides / Q000378:metabolism* / Q000494:pharmacology; D008745:Methylation / Q000187:drug effects; D005810:Multigene Family; D009943:Organophosphorus Compounds / Q000378:metabolism* / Q000494:pharmacology; D013302:Streptomyces / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D006540:Herbicides; D009943:Organophosphorus Compounds; C003122:bialaphos