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Isolation of DD carboxypeptidase from Streptomyces albus G culture filtrates.

作者信息

Ghuysen J M, Leyh-Bouille M, Bonaly R, Nieto M, Perkins H R, Schleifer K H, Kandler O

出版信息

Biochemistry. 1970 Jul 21;9(15):2955-61. doi: 10.1021/bi00817a004.

DOI:10.1021/bi00817a004
PMID:4919965
Abstract
摘要

相似文献

1
Isolation of DD carboxypeptidase from Streptomyces albus G culture filtrates.
Biochemistry. 1970 Jul 21;9(15):2955-61. doi: 10.1021/bi00817a004.
2
Substrate requirements of the Streptomyces albus G DD carboxypeptidase.白色链霉菌G型DD羧肽酶的底物需求
Biochemistry. 1970 Jul 21;9(15):2961-70. doi: 10.1021/bi00817a005.
3
Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.来自链霉菌菌株R 61的青霉素敏感型DD-羧肽酶
Biochemistry. 1971 May 25;10(11):2163-70. doi: 10.1021/bi00787a032.
4
[Isolation and properties of carboxypeptidase from Streptomyces spheroides, strain 35].
Biokhimiia. 1987 Dec;52(12):2002-8.
5
The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties.来自白色链霉菌G的胞外DD-羧肽酶-内肽酶。纯化及化学性质。
Biochem J. 1978 Dec 1;175(3):793-800. doi: 10.1042/bj1750793.
6
Peptide inhibitors of Streptomyces DD-carboxypeptidases.链霉菌DD-羧肽酶的肽类抑制剂。
Biochem J. 1973 Jan;131(1):163-71. doi: 10.1042/bj1310163.
7
D-D carboxypeptidase activity in Escherichia coli K 12.大肠杆菌K12中的D- D羧肽酶活性
Biochimie. 1973;55(9):1175-8. doi: 10.1016/s0300-9084(73)80460-2.
8
Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase--transpeptidase for peptide acceptors.链霉菌R39细胞壁肽聚糖的结构及其胞外DD-羧肽酶-转肽酶对肽受体的特异性谱
Biochemistry. 1973 Mar 27;12(7):1243-51. doi: 10.1021/bi00731a001.
9
The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G. Interaction with beta-lactam antibiotics.白色链霉菌G的胞外DD-羧肽酶-内肽酶。与β-内酰胺抗生素的相互作用。
Biochem J. 1978 Dec 1;175(3):801-5. doi: 10.1042/bj1750801.
10
On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin.关于青霉素、万古霉素和瑞斯托菌素对白链霉菌G D-羧肽酶的作用机制。
Biochemistry. 1970 Jul 21;9(15):2971-5. doi: 10.1021/bi00817a006.

引用本文的文献

1
The exocellular beta-lactamase of Streptomyces albus G. Purification, properties and comparison with the exocellular DD-carboxypeptidase.白色链霉菌G的胞外β-内酰胺酶。纯化、性质及与胞外DD-羧肽酶的比较。
Biochem J. 1981 Jan 1;193(1):75-82. doi: 10.1042/bj1930075.
2
Modifications of the acyl-D-alanyl-D-alanine terminus affecting complex-formation with vancomycin.影响与万古霉素形成复合物的酰基-D-丙氨酰-D-丙氨酸末端修饰
Biochem J. 1971 Aug;123(5):789-803. doi: 10.1042/bj1230789.
3
Homoserine and diaminobutyric acid in the mucopeptide-precursor-nucleotides and cell walls of some plant-pathogenic corynebacteria.
某些植物病原棒状杆菌的粘肽前体核苷酸及细胞壁中的高丝氨酸和二氨基丁酸
Biochem J. 1971 Feb;121(3):417-23. doi: 10.1042/bj1210417.
4
Fluorescence and circular dichroism studies on the Streptomyces R61 DD-carboxypeptidase-transpeptidase. Penicillin binding by the enzyme.链霉菌R61 D-羧肽酶-转肽酶的荧光和圆二色性研究。该酶与青霉素的结合。
Biochem J. 1973 Nov;135(3):493-505. doi: 10.1042/bj1350493.
5
Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.作为转肽酶的链霉菌DD-羧肽酶。对充当羧基受体的氨基化合物的特异性。
Biochem J. 1973 Apr;131(4):707-18. doi: 10.1042/bj1310707.
6
Peptide inhibitors of Streptomyces DD-carboxypeptidases.链霉菌DD-羧肽酶的肽类抑制剂。
Biochem J. 1973 Jan;131(1):163-71. doi: 10.1042/bj1310163.
7
Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.青霉素与细菌细胞的相互作用:青霉素结合蛋白和青霉素敏感酶。
Bacteriol Rev. 1974 Sep;38(3):291-335. doi: 10.1128/br.38.3.291-335.1974.
8
Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.
Proc Natl Acad Sci U S A. 1972 Mar;69(3):662-6. doi: 10.1073/pnas.69.3.662.
9
Exocellular beta-lactamases of Streptomyces albus G and strains R39 and K11.白色链霉菌G以及R39和K11菌株的胞外β-内酰胺酶
Antimicrob Agents Chemother. 1973 Feb;3(2):289-98. doi: 10.1128/AAC.3.2.289.
10
Role of the penicillin-sensitive transpeptidation reaction in attachment of newly synthesized peptidoglycan to cell walls of Micrococcus luteus.青霉素敏感转肽反应在新合成的肽聚糖附着于藤黄微球菌细胞壁中的作用。
Proc Natl Acad Sci U S A. 1972 Nov;69(11):3355-9. doi: 10.1073/pnas.69.11.3355.