Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus.
作者信息
Yocum R R, Blumberg P M, Strominger J L
出版信息
J Biol Chem. 1974 Aug 10;249(15):4863-71.
PMID:4211099
Abstract
摘要
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Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus.嗜热脂肪芽孢杆菌膜中嗜热D-丙氨酸羧肽酶的纯化与特性分析
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D-alanine carboxypeptidase from Bacillus subtilis membranes. I. Purification and characterization.来自枯草芽孢杆菌膜的D-丙氨酸羧肽酶。I. 纯化与特性鉴定。
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D-alanine carboxypeptidases of Bacillus stearothermophilus: solubilisation of particulate enzymes and mechanism of action of penicillin.嗜热脂肪芽孢杆菌的D-丙氨酸羧肽酶：颗粒酶的溶解及青霉素的作用机制
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D-alanine carboxypeptidase from Bacillus subtilis membranes. II. Interaction with penicillins and cephalosporins.来自枯草芽孢杆菌膜的D-丙氨酸羧肽酶。II. 与青霉素和头孢菌素的相互作用。
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Transpeptidases and D,D-carboxypeptidases in bacilli.芽孢杆菌中的转肽酶和D，D-羧肽酶
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Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose.通过与琼脂糖共价偶联的6-氨基青霉烷酸对枯草芽孢杆菌膜结合D-丙氨酸羧肽酶的抑制作用。
J Bacteriol. 1974 Feb;117(2):783-5. doi: 10.1128/jb.117.2.783-785.1974.
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Limited proteolysis of the penicillin-sensitive D-alanine carboxypeptidase purified from Bacillus subtilis membranes. Active water-soluble fragments generated by cleavage of a COOH-terminal membrane anchor.对从枯草芽孢杆菌膜中纯化的青霉素敏感的D-丙氨酸羧肽酶进行有限的蛋白酶解。通过切割COOH末端膜锚产生活性水溶性片段。
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[Characterization and separation of exocellular gamma-D-glutamyl-(L)meso-diaminopimelate endopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602].[球形芽孢杆菌9602胞外γ-D-谷氨酰-(L)-内消旋二氨基庚二酸内肽酶和LD-羧肽酶的表征与分离]
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Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.嗜热脂肪芽孢杆菌的D-丙氨酸羧肽酶将青霉素G降解为苯乙酰甘氨酸。
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Utilization of a depsipeptide substrate for trapping acyl-enzyme intermediates of penicillin-sensitive D-alanine carboxypeptidases.利用一种缩肽底物捕获青霉素敏感的D-丙氨酸羧肽酶的酰基-酶中间体。
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Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12.在大肠杆菌K12突变体中同时缺失D-丙氨酸羧肽酶IB-C和青霉素结合成分IV。
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Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.青霉素作用机制：青霉素和底物在两种细菌D-丙氨酸羧肽酶中与同一个活性位点丝氨酸共价结合。
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