| 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. | |
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MedLine Citation:
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PMID: 729579 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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W P Hammes |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 91 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1978 Nov |
Date Detail:
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Created Date: 1979-03-13 Completed Date: 1979-03-13 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY, WEST |
Other Details:
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Languages: eng Pagination: 501-7 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Carboxypeptidases
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metabolism* Cell Membrane / enzymology Cell Wall / metabolism Glycine Kinetics Muramic Acids Peptidoglycan / biosynthesis* Stereoisomerism Streptococcaceae / enzymology* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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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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