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对氨基苯甲酸合酶的化学修饰。

Chemical modification of PABA synthase.

作者信息

McLeish M J, Caine J M

机构信息

School of Pharmaceutical Chemistry, Victorian College of Pharmacy (Monash University) Ltd., Parkville.

出版信息

Biochem Int. 1991 Aug;24(6):1033-42.

PMID:1781781
Abstract

p-Aminobenzoic acid (PABA) synthase catalyses the first step in folic acid biosynthesis, the conversion of chorismate to p-aminobenzoate. In general, difficulties in purification have permitted only limited investigation of this enzyme. However, in an attempt to identify possible active site residues, the E. coli enzyme has been incubated with a range of protein modifying agents. Results indicate that cysteine, histidine, arginine and tyrosine residues are important for enzyme activity. Attempts were made to determine the subunits upon which these residues were located.

摘要

对氨基苯甲酸(PABA)合酶催化叶酸生物合成的第一步,即分支酸转化为对氨基苯甲酸。一般来说,由于纯化困难,对这种酶的研究非常有限。然而,为了确定可能的活性位点残基,已将大肠杆菌中的这种酶与一系列蛋白质修饰剂一起孵育。结果表明,半胱氨酸、组氨酸、精氨酸和酪氨酸残基对酶活性很重要。研究人员试图确定这些残基所在的亚基。

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