Biosynthesis of the Peptidoglycan of Bacterial Cell Walls XIV. PURIFICATION AND PROPERTIES OF TWO d-ALANINE CARBOXYPEPTIDASES FROM ESCHERICHIA COLI
作者： K Izaki , J L Strominger
DOI: 10.1016/S0021-9258(18)93394-6
关键词: Uridine 、 Biochemistry 、 Pentapeptide repeat 、 Bacterial cell structure 、 Escherichia coli 、 Enzyme 、 Peptidoglycan 、 Biosynthesis 、 Carboxypeptidase 、 Biology
摘要: Abstract d-Alanine carboxypeptidase I, which removes the terminal d-alanine residue of uridine nucleotide, UDP-N-acetylmuramyl pentapeptide, and several related compounds occurs in both particulate soluble fractions Escherichia coli other gram-negative bacteria. The enzyme has been purified 120-fold some its properties are reported. is competitively inhibited by penicillins cephalosporins at very low concentrations. II, catalyzes hydrolysis penultimate nucleotide substrate, also separated from I. This not cephalosporins. possible physiological substrate function these enzymes discussed.
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