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首页> 外文期刊>Infection and immunity >Some properties of a D-alanine carboxypeptidase in envelope fractions of Neisseria gonorrhoeae.
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Some properties of a D-alanine carboxypeptidase in envelope fractions of Neisseria gonorrhoeae.

机译：Neisseria淋病囊腔包络分数D-丙氨酸羧肽酶的一些性质。

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摘要

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.
机译：Neisseria淋病菌株GC1（稳定，凸起的中间菌落形态菌株）和T1型具有D-丙氨酸羧肽酶，其释放来自尿苷5'-二磷酸 - N-乙酰胺肽肽的末端丙氨酸残基（从芽孢杆菌中分离）米羚羊。 GC1包络的D-丙氨酸羧肽酶在pH8.0至10.0之间具有宽的pH值。当改变Tris（羟甲基）氨基甲烷缓冲液的摩尔性时，当存在20至80mM Mg2 +时，活性显示出0.2至0.4米的最佳活动。当存在20至80mM mg2 +时，活性较高（135％的对照水平）。酶的km为0.25毫米。通过几种β-内酰胺抗生素抑制D-丙氨酸羧肽酶，50％抑制水平为10（-8）M青霉素G,10（-8）氨氨苄青霉素，10（-5）M克罗克林素，5×10（ -7）M甲氧西林。

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