Hidaka T, Imai S, Hara O, Anzai H, Murakami T, Nagaoka K, Seto H
Institute of Applied Microbiology, University of Tokyo, Japan.
J Bacteriol. 1990 Jun;172(6):3066-72. doi: 10.1128/jb.172.6.3066-3072.1990.
An enzyme catalyzing the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos (BA) was isolated from the cell extract of a mutant (NP71) of Streptomyces hygroscopicus SF1293. This enzyme, carboxyphosphonoenolpyruvate (CPEP) phosphonomutase, was first identified as a protein lacking in a mutant (NP213) defective in one of the steps in the pathway to BA. The first 30 residues of the amino terminus of this protein were identical to those predicted by the nucleotide sequence of the gene that restored BA production to NP213. The substrate of the enzyme, a P-carboxylated derivative of phosphoenolpyruvate named CPEP, was also isolated from the broth filtrate of NP213 as a new biosynthetic intermediate of BA. CPEP phosphonomutase catalyzes the rearrangement of the carboxyphosphono group of CPEP to form the C-P bond of phosphinopyruvate.
从吸水链霉菌SF1293的突变体（NP71）的细胞提取物中分离出一种催化形成异常C-P键的酶，该键参与抗生素双丙氨膦（BA）的生物合成。这种酶，即羧基膦酰烯醇丙酮酸（CPEP）膦酸变位酶，最初是在BA合成途径中某一步骤有缺陷的突变体（NP213）中被鉴定为一种缺失的蛋白质。该蛋白质氨基末端的前30个残基与恢复NP213的BA生产的基因的核苷酸序列预测的残基相同。该酶的底物，一种名为CPEP的磷酸烯醇丙酮酸的P-羧化衍生物，也从NP213的肉汤滤液中分离出来，作为BA的一种新的生物合成中间体。CPEP膦酸变位酶催化CPEP的羧基膦酰基重排，形成膦酰丙酮酸的C-P键。
