Formation of 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid during cleavage of penicillin G by D-alanine carboxypeptidase from Bacillus stearothermophilus.
作者信息
Hammarström S, Strominger J L
出版信息
J Biol Chem. 1976 Dec 25;251(24):7947-9.
PMID:1002716
Abstract
摘要
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Formation of 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid during cleavage of penicillin G by D-alanine carboxypeptidase from Bacillus stearothermophilus.
J Biol Chem. 1976 Dec 25;251(24):7947-9.
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Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.
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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.
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The mechanism of action of penicillin. Penicillin acylates the active site of Bacillus stearothermophilus D-alanine carboxypeptidase.
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Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus.
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