首页> 外文期刊>The Journal of Antibiotics: An International Journal >STUDIES ON THE BIOSYNTHESIS OF BIALAPHOS - BIOCHEMICAL MECHANISM OF C-P BOND FORMATION - DISCOVERY OF PHOSPHONOPYRUVATE DECARBOXYLASE WHICH CATALYZES THE FORMATION OF PHOSPHONOACETALDEHYDE FROM PHOSPHONOPYRUVATE
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STUDIES ON THE BIOSYNTHESIS OF BIALAPHOS - BIOCHEMICAL MECHANISM OF C-P BOND FORMATION - DISCOVERY OF PHOSPHONOPYRUVATE DECARBOXYLASE WHICH CATALYZES THE FORMATION OF PHOSPHONOACETALDEHYDE FROM PHOSPHONOPYRUVATE

机译:双酰脲的生物合成-C-P键形成的生物化学机理-磷酸丙酮酸脱羧酶催化磷酸丙酮酸脱羧酶的发现

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摘要

The biosynthetic step following the phosphoenolpyruvate (PEP) phosphomutase reaction which forms a C-P bond of bialaphos was proven by the identification of phosphonopyruvate (PnPy) and phosphonoacetaldehyde (PnAA) as intermediates in the culture broth of Streptomyces hygroscopicus, a producing organism of bialaphos, and by detection of enzymatic decarboxylation of PnPy to PnAA. Purified PnPy decarboxylase turned out to require thiamine diphosphate and Mg2+ as cofactors. PnPy decarboxylase drives the unfavorable forward reaction to form PnPy catalyzed by PEP phosphomutase and is suggested to be essential to C-P compound biosynthesis. [References: 30]
机译:磷酸烯醇丙酮酸(PEP)磷酸突变酶反应形成了双丙氨膦的CP键后的生物合成步骤已通过鉴定膦酰丙酮酸(PnPy)和膦酰乙醛(PnAA)作为吸水链霉菌的培养液中的中间体而得到证实,该链霉菌是产生双丙氨酸的生物,并且通过检测PnPy酶促脱羧为PnAA。纯化的PnPy脱羧酶证明需要硫胺素二磷酸和Mg2 +作为辅助因子。 PnPy脱羧酶驱动PEP磷酸变位酶催化不利的正向反应形成PnPy,并被认为对C-P化合物的生物合成至关重要。 [参考:30]

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