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链霉菌DD-羧肽酶的肽类抑制剂。

Peptide inhibitors of Streptomyces DD-carboxypeptidases.

作者信息

Nieto M, Perkins H R, Leyh-Bouille M, Frère J M, Ghuysen J M

出版信息

Biochem J. 1973 Jan;131(1):163-71. doi: 10.1042/bj1310163.

Abstract
  1. Peptides that inhibit the dd-carboxypeptidases from Streptomyces strains albus G and R61 were synthesized. They are close analogues of the substrates of these enzymes. The enzymes from albus G and R61 strains are in general inhibited by the same peptides, but the enzyme from strain R39 differs considerably. 2. The two C-terminal residues of the peptide substrates and inhibitors appear to be mainly responsible for the initial binding of the substrate to the enzymes from albus G and R61 strains. The side chain in the third residue from the C-terminus seems critical in inducing catalytic activity. 3. Experimental evidence is presented suggesting that the amide bond linking the two C-terminal residues has a cis configuration when bound to the enzymes from strains albus G and R61. 4. The peptide inhibitors are not antibiotics against the same micro-organisms.
摘要
  1. 合成了抑制来自白色链霉菌G菌株和R61菌株的双功能羧肽酶的肽。它们是这些酶底物的类似物。来自白色链霉菌G菌株和R61菌株的酶通常被相同的肽抑制,但来自R39菌株的酶有很大差异。2. 肽底物和抑制剂的两个C末端残基似乎主要负责底物与来自白色链霉菌G菌株和R61菌株的酶的初始结合。C末端第三个残基的侧链在诱导催化活性方面似乎至关重要。3. 实验证据表明,连接两个C末端残基的酰胺键在与来自白色链霉菌G菌株和R61菌株的酶结合时具有顺式构型。4. 肽抑制剂对相同的微生物不是抗生素。

相似文献

6
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.

引用本文的文献

本文引用的文献

1
Energetics of peptide formation.肽形成的能量学
Nature. 1952 May 31;169(4309):922. doi: 10.1038/169922a0.

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