Document Detail

The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of D-amino acids or glycine on the formation of wall-bound peptidoglycan.
MedLine Citation:
PMID:  729579     Owner:  NLM     Status:  MEDLINE    
The effects in vitro of D-amino acids or glycine on the formation of wall-bound peptidoglycan were studied with wall membrane enzyme preparations from Gaffkya homari. These amino acids inhibited the incorporation of nascent peptidoglycan into the preformed polymer (e.g. ID50 values for D-alanine, D-leucine, and glycine = 5.6 mmol/l, 1.3 mmol/l, and 11 mmol/l, respectively). The inhibition was accompanied by an incorporation of the inhibitor into position 4 of the peptide subunit Ala1-DGlu2(Lys3-DAla4), where the indices refer to the position of an amino acid residue within the peptide subunit. It is suggested that the reaction is catalyzed by an LD-carboxypeptidase. Therefore, this enzyme has also D-amino acid exchange activity. At inhibitory concentration fewer tripeptide subunits were formed in the nascent peptidoglycan in favour of the formation of tetrapeptide subunits bearing the inhibitor at the C termini. The tripeptide subunits are assumed to be necessary in order that nascent peptidoglycan is utilized as substrate in the transpeptidation reaction. Thus an essential role of the LD-carboxypeptidase is indicated.
W P Hammes
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  91     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1978 Nov 
Date Detail:
Created Date:  1979-03-13     Completed Date:  1979-03-13     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  501-7     Citation Subset:  IM    
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MeSH Terms
Carboxypeptidases / metabolism*
Cell Membrane / enzymology
Cell Wall / metabolism
Muramic Acids
Peptidoglycan / biosynthesis*
Streptococcaceae / enzymology*
Substrate Specificity
Reg. No./Substance:
0/Muramic Acids; 0/Peptidoglycan; 56-40-6/Glycine; EC 3.4.-/Carboxypeptidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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