Syntheses of the P-methylase substrates of the bialaphos biosynthetic pathway.
Genetic studies suggest that either N-acetyldemethyl phosphinothricin (1, N-AcDMPT) or N-acetyldemethyl phosphinothricin tripeptide (2, N-AcDMPTT) is the substrate for the P-methylation reaction in the biosynthesis of phosphinothricin tripeptide (PTT), which is widely used as an herbicide. To study the mechanism for this unique P-methylation reaction catalyzed by the BcpD protein and the functions of the unusual nonribosomal peptide synthetases involved in PTT biosynthesis, this work reports the chemical syntheses of 1 and 2.
Xiao
Youli
Y
Department of Chemistry, Boston University, Boston, Massachusetts 02215, USA.
Lee
Kent
K
Liu
Pinghua
P
D000613:Aminobutyrates / Q000138:chemical synthesis* / Q000737:chemistry; D006540:Herbicides / Q000138:chemical synthesis* / Q000737:chemistry; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D063065:Organophosphonates / Q000737:chemistry; D009943:Organophosphorus Compounds / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D013302:Streptomyces / Q000737:chemistry / Q000378:metabolism*
D000613:Aminobutyrates; D006540:Herbicides; D009842:Oligopeptides; D063065:Organophosphonates; D009943:Organophosphorus Compounds; C046087:N-acetyldemethylphosphinothricin; C003122:bialaphos; D008780:Methyltransferases; C094206:P-methyltransferase