荧光假单胞菌23F中一种不依赖磷饥饿的碳-磷键裂解活性的体外特性研究
In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F.
作者信息
McMullan G, Quinn J P
机构信息
School of Biology and Biochemistry, Queen's University, Belfast, Northern Ireland.
出版信息
J Bacteriol. 1994 Jan;176(2):320-4. doi: 10.1128/jb.176.2.320-324.1994.
Abstract
A novel, metal-dependent, carbon-phosphorus bond cleavage activity, provisionally named phosphonoacetate hydrolase, was detected in crude extracts of Pseudomonas fluorescens 23F, an environmental isolate able to utilize phosphonoacetate as the sole carbon and phosphorus source. The activity showed unique specificity toward this substrate; its organic product, acetate, was apparently metabolized by the glyoxylate cycle enzymes of the host cell. Unlike phosphonatase, which was also detected in crude extracts of P. fluorescens 23F, phosphonoacetate hydrolase was inducible only in the presence of its sole substrate and did not require phosphate starvation.
摘要
在荧光假单胞菌23F（一种能够利用膦酰基乙酸作为唯一碳源和磷源的环境分离菌株）的粗提物中，检测到一种新型的、依赖金属的碳-磷键裂解活性，暂命名为膦酰基乙酸水解酶。该活性对这种底物表现出独特的特异性；其有机产物乙酸显然是由宿主细胞的乙醛酸循环酶代谢的。与在荧光假单胞菌23F粗提物中也检测到的磷酸酶不同，膦酰基乙酸水解酶仅在其唯一底物存在时才可诱导，并且不需要磷酸盐饥饿条件。
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