马杜拉放线菌R39胞外DD-羧肽酶-转肽酶中的青霉素结合位点。
The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.
作者信息
Duez C, Joris B, Frère J M, Ghuysen J M, Van Beeumen J
出版信息
Biochem J. 1981 Jan 1;193(1):83-6. doi: 10.1042/bj1930083.
Abstract
Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In contrast, the native benzylpenicilloyl-enzyme complex is very stable (half-life 70 h at 37 degrees C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frère, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-629].
摘要
先前在苄青霉素与马杜拉放线菌R39的胞外DD - 羧肽酶 - 转肽酶之间形成的复合物经热变性和链霉蛋白酶降解后，产生一种七肽H - 亮氨酸 - 脯氨酸 - 丙氨酸 - 丝氨酸 - 天冬酰胺 - 甘氨酸 - 缬氨酸 - 羟基，其中苄青霉素酰基以酯键连接到丝氨酸残基上。这种连接非常不稳定，其水解会导致苄青霉素酸的释放。相比之下，天然的苄青霉素酰 - 酶复合物非常稳定（在37℃下半衰期为70小时），其分解是通过结合的苄青霉素酰基的断裂进行的[富阿德、弗雷尔、居伊森、迪兹和岩津保（1976年）《生物化学杂志》155卷，623 - 629页]。
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Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):309-19. doi: 10.1098/rstb.1980.0048.
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Chemical studies on methionyl-tRNA synthetase from Escherichia coli.大肠杆菌甲硫氨酰 - tRNA合成酶的化学研究。
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Sequence analysis of fluorescamine-stained peptides and proteins purified on a nanomole scale. Application to proteins of bacteriophage MS2.对荧光胺染色的、在纳摩尔规模上纯化的肽和蛋白质进行序列分析。应用于噬菌体MS2的蛋白质。
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Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis.通过凝胶电泳对纳摩尔级纯化的蛋白质进行氨基末端序列分析。
J Biol Chem. 1972 May 25;247(10):3242-51.
6
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7
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8
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9
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10
NMR evidence for the structure of the complex between penicillin and the DD-carboxypeptidase of Streptomyces R61.核磁共振（NMR）证据表明青霉素与链霉菌R61的DD - 羧肽酶之间复合物的结构。
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