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PMID: 4772272 Published · ppublish English Journal Article

Molecular weight and amino acid composition of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.

The Biochemical journal ·Vol. 135 ·No. 3 ·1973-11-00 ·Pages 463-8

Frère JM, Ghuysen JM, Perkins HR, Nieto M

Abstract

A procedure allowing the purification of milligram amounts of the exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R61 to protein homogeneity (95% purity) is described. The isolated protein has a molecular weight of about 38000 and consists of one polypeptide chain. Its amino acid composition is presented.

MeSH Terms
Acyltransferases/analysis,isolation & purification Amino Acid Sequence Carboxypeptidases/analysis,isolation & purification Electrophoresis, Polyacrylamide Gel Isoelectric Focusing Molecular Weight Peptidoglycan Proteins/analysis Streptomyces/enzymology
Chemicals
Peptidoglycan Proteins Acyltransferases Carboxypeptidases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Frère J M
Ghuysen J M
Perkins H R
Nieto M
References (10)
10 references, click to expand
  1. Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of streptomyces R61.
    Biochem J. 1973 Nov;135(3):483-92 PMID: 4772274
  2. Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11.
    Biochemistry. 1972 Mar 28;11(7):1290-8 PMID: 5012980
  3. Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.
    Biochemistry. 1971 May 25;10(11):2163-70 PMID: 4998135
  4. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
    J Biol Chem. 1969 Aug 25;244(16):4406-12 PMID: 5806584
  5. Fluorescence and circular dichroism studies on the Streptomyces R61 DD-carboxypeptidase-transpeptidase. Penicillin binding by the enzyme.
    Biochem J. 1973 Nov;135(3):493-505 PMID: 4772275
  6. The oxidation of ribonuclease with performic acid.
    J Biol Chem. 1956 Apr;219(2):611-21 PMID: 13319283
  7. Peptide inhibitors of Streptomyces DD-carboxypeptidases.
    Biochem J. 1973 Jan;131(1):163-71 PMID: 4722034
  8. Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.
    Proc Natl Acad Sci U S A. 1972 Mar;69(3):662-6 PMID: 4501580
  9. Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.
    Biochem J. 1973 Apr;131(4):707-18 PMID: 4722450
  10. DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.
    Antimicrob Agents Chemother. 1973 Feb;3(2):181-7 PMID: 4790585
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1350463
Published
1973-11-00
Pages
463-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1165848
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1350463 PMC Full Text View journal details
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