大肠杆菌青霉素结合蛋白5和6同时释放青霉噻唑酸和苯乙酰甘氨酸。
Simultaneous release of penicilloic acid and phenylacetyl glycine by penicillin-binding proteins 5 and 6 of Escherichia coli.
作者信息
Amanuma H, Strominger J L
出版信息
J Bacteriol. 1984 Nov;160(2):822-3. doi: 10.1128/jb.160.2.822-823.1984.
Abstract
Penicillin-binding proteins (PBPs) 5 and 6 of Escherichia coli released the bound penicilloyl moiety at an intermediate rate relative to, e.g., Staphylococcus aureus PBPs 4 (rapid) and 1 or 2 (slow). Each of these E. coli PBPs released the bound penicilloyl moiety as both penicilloic acid (hydrolysis) and phenylacetyl glycine (scission of the C-5--C-6 bond followed by hydrolysis).
摘要
大肠杆菌的青霉素结合蛋白（PBPs）5和6释放结合的青霉噻唑基团的速率处于中间水平，相对于例如金黄色葡萄球菌的PBPs 4（快速）和1或2（缓慢）而言。这些大肠杆菌PBPs中的每一个都以青霉酸（水解）和苯乙酰甘氨酸（C-5-C-6键断裂后水解）的形式释放结合的青霉噻唑基团。
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Simultaneous release of penicilloic acid and phenylacetyl glycine by penicillin-binding proteins 5 and 6 of Escherichia coli.大肠杆菌青霉素结合蛋白5和6同时释放青霉噻唑酸和苯乙酰甘氨酸。
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本文引用的文献
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2
Penicillin-binding proteins and the mechanism of action of beta-lactam antibiotics.青霉素结合蛋白与β-内酰胺类抗生素的作用机制
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Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39.与链霉菌R61和R39的胞外DD-羧肽酶-转肽酶相互作用后苄青霉素的碎片化
Nature. 1975 Nov 13;258(5531):168-70. doi: 10.1038/258168a0.
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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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