Stability of D-5,5-dimethyl-delta2-thiazoline-4-carboxylic acid in relation to its possible occurrence as a degradation product of penicillin by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and the membrane-bound dd-carboxypeptidase from Bacillus stearothermophilus.-Reference-Cited by-同舟云学术

Stability of D-5,5-dimethyl-delta2-thiazoline-4-carboxylic acid in relation to its possible occurrence as a degradation product of penicillin by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and the membrane-bound dd-carboxypeptidase from Bacillus stearothermophilus.

Published:1978-05 Issue:10 Volume:253 Page:3660-3665
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Adriaens P.,Meesschaert B.,Frère J.M.,Vanderhaeghe H.,Degelaen J.,Ghuysen J.M.,Eyssen H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference15 articles.

1. The Bacterial DD-Carboxypeptidase-Transpeptidase Enzyme System. A New Insight Into the Mode of Action of Penicillin;Ghuysen,1977

2. The Concept of the Penicillin Target from 1965 until Today: The Thirteenth Marjory Stephenson Memorial Lecture

3. Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39

4. Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61

5. Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.

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