The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G. Interaction with beta-lactam antibiotics.
Kinetically, the three-step model proposed for the interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidases-transpeptidases of Streptomyces R61 and Actinomadura R39 [Frère, Ghuysen & Iwatsubo (1975) Eur. J. Biochem. 57, 343--357; Fuad, Frère, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623--629] applies to the interaction between the much less penicillin-sensitive exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G and at least phenoxymethylpenicillin, cephalothin and cephalosporin C. The penicillin resistance of the albus G enzyme is mainly due to the low efficiency with which the first reversible complex formed with the antibiotic (complex EI) undergoes transformation into a second more stable complex EI*. Analysis of the ternary interaction between enzyme, NalphaNepsilon-diacetyl-L-lysyl-D-alanyl-D-alanine (Ac2-L-Lys-D-Ala-D-Ala) and cephalosporin C indicates a non-competitive mechanism.
11 references, click to expand
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Exocellular DD-carboxypeptidases-transpeptidases from Streptomyces.Methods Enzymol. 1976;45:610-36 PMID: 1012018
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On the mechanism of action of antibiotics which act as irreversible enzyme inhibitors.Biochem Pharmacol. 1975 Jun 15;24(11-12):1153-60 PMID: 1137602
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Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics. A choice of models.Eur J Biochem. 1975 Sep 15;57(2):343-51 PMID: 1175647
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Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39.Nature. 1975 Nov 13;258(5531):168-70 PMID: 1186898
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Interaction between penicillin and the DD-carboxypeptidase of the unstable L-form of Proteus mirabilis strain 19.Eur J Biochem. 1978 Apr 17;85(2):325-30 PMID: 348468
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On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin.Biochemistry. 1970 Jul 21;9(15):2971-5 PMID: 5474798
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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.J Biol Chem. 1978 May 25;253(10):3660-5 PMID: 649594
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The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties.Biochem J. 1978 Dec 1;175(3):793-800 PMID: 743235
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Purification of the membrane-bound DD-carboxypeptidase of the unstable spheroplast L-form of Proteus mirabilis by affinity chromatography. Non-competitive inhibition of the enzyme by penicillins and low stability of the enzyme-inhibitor complex.Eur J Biochem. 1976 Dec 11;71(2):585-93 PMID: 795672
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Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.Nature. 1976 Apr 1;260(5550):451-4 PMID: 815828
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Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase--transpeptidase from Streptomyces R39.Biochem J. 1976 Jun 1;155(3):623-9 PMID: 949323
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