doi: 10.1073/pnas.72.9.3463.
Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus
- PMID: 1059132
- PMCID: PMC433014
- DOI: 10.1073/pnas.72.9.3463
Item in Clipboard
Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus
Proc Natl Acad Sci U S A.
1975 Sep.
Abstract
D-Alanine carboxypeptidase from Bacillus stearothermophilus is a membrane-bound enzyme which is inhibited by covalent interaction with penicillin G. The penicilloyl enzyme spontaneously reactivates and simultaneously releases a penicillin G degradation product; 0.2 mumol of the latter was isolated after incubation of 4.2 mumol of [8-14C]penicillin G with 10 g of membrane protein. It was identified as phenylacetylglycine by chromatographic techniques, infrared spectroscopy, and mass spectrometry. A mechanism for the degradation is proposed in which the remaining part of penicillin G would be released as 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid. The implications of this finding are discussed.
Similar articles
-
Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12. doi: 10.1073/pnas.74.3.1009. Proc Natl Acad Sci U S A. 1977. PMID: 403523 Free PMC article.
-
Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.Proc Natl Acad Sci U S A. 1979 Jun;76(6):2730-4. doi: 10.1073/pnas.76.6.2730. Proc Natl Acad Sci U S A. 1979. PMID: 111240 Free PMC article.
-
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. J Biol Chem. 1976. PMID: 1002716 No abstract available.
-
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. J Biol Chem. 1978. PMID: 649594
-
Hydroxylaminolysis of penicillin binding componenets is enzymatically catalyzed.J Biol Chem. 1977 Nov 10;252(21):7525-9. J Biol Chem. 1977. PMID: 410805
Cited by
-
Simultaneous release of penicilloic acid and phenylacetyl glycine by penicillin-binding proteins 5 and 6 of Escherichia coli.J Bacteriol. 1984 Nov;160(2):822-3. doi: 10.1128/jb.160.2.822-823.1984. J Bacteriol. 1984. PMID: 6094494 Free PMC article.
-
Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12. doi: 10.1073/pnas.74.3.1009. Proc Natl Acad Sci U S A. 1977. PMID: 403523 Free PMC article.
-
Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.Proc Natl Acad Sci U S A. 1979 Jun;76(6):2730-4. doi: 10.1073/pnas.76.6.2730. Proc Natl Acad Sci U S A. 1979. PMID: 111240 Free PMC article.
-
Penem derivatives: beta-lactamase stability and affinity for penicillin-binding proteins in Escherichia coli.Antimicrob Agents Chemother. 1982 Mar;21(3):492-7. doi: 10.1128/AAC.21.3.492. Antimicrob Agents Chemother. 1982. PMID: 7049076 Free PMC article.
-
A point mutation leads to altered product specificity in beta-lactamase catalysis.Proc Natl Acad Sci U S A. 1997 Jan 21;94(2):443-7. doi: 10.1073/pnas.94.2.443. Proc Natl Acad Sci U S A. 1997. PMID: 9012802 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
