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淋病奈瑟菌包膜组分中D-丙氨酸羧肽酶的某些特性

Some properties of a D-alanine carboxypeptidase in envelope fractions of Neisseria gonorrhoeae.

作者信息

Davis R H, Salton M R

出版信息

Infect Immun. 1975 Nov;12(5):1065-9. doi: 10.1128/iai.12.5.1065-1069.1975.

DOI:10.1128/iai.12.5.1065-1069.1975

PMID:332

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC415398/

Abstract

Envelope preparations of Neisseria gonorrhoeae strain GC1 (a stable, piliated strain of intermediate colony morphology) and type T1 possess a D-alanine carboxypeptidase which releases the terminal alanine residue from the uridine 5'-diphosphate-N-acetyl muramylpentapeptide substrate (isolated from Bacillus cereus T). The D-alanine carboxypeptidase of the GC1 envelopes has a broad pH optimum between pH 8.0 to 10.0. When the molarity of the tris(hydroxymethyl)aminomethane buffer was varied, the activity showed an optimum over the range 0.2 to 0.4 M. Activity was higher (135% of control level) when 20 to 80 mM Mg2+ was present. The Km for the enzyme was 0.25 mM. The D-alanine carboxypeptidase was inhibited by several beta-lactam antibiotics and the 50% inhibitory levels were 10(-8) M penicillin G, 10(-8) M ampicillin, 10(-5) M cloxacillin, and 5 x 10(-7) M methicillin.

摘要

淋病奈瑟菌GC1菌株（一种具有中等菌落形态的稳定、有菌毛菌株）和T1型的包膜制剂含有一种D-丙氨酸羧肽酶，该酶可从尿苷5'-二磷酸-N-乙酰胞壁酰五肽底物（从蜡样芽孢杆菌T中分离）释放末端丙氨酸残基。GC1包膜的D-丙氨酸羧肽酶在pH 8.0至10.0之间具有较宽的最适pH值。当三（羟甲基）氨基甲烷缓冲液的摩尔浓度变化时，活性在0.2至0.4 M范围内显示出最佳值。当存在20至80 mM Mg2+时，活性更高（为对照水平的135%）。该酶的Km为0.25 mM。D-丙氨酸羧肽酶受到几种β-内酰胺抗生素的抑制，50%抑制水平分别为：青霉素G 10^(-8) M、氨苄西林10^(-8) M、氯唑西林10^(-5) M和甲氧西林5×10^(-7) M。