Abstract
A gene, mpl, encoding UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelat e ligase was recognized by its amino acid sequence homology with murC as the open reading frame yjfG present at 96 min on the Escherichia coli map. The existence of such an enzymatic activity was predicted from studies indicating that reutilization of the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate occurred and accounted for well over 30% of new cell wall synthesis. Murein tripeptide ligase activity could be demonstrated in crude extracts, and greatly increased activity was produced when the gene was cloned and expressed under control of the trc promoter. A null mutant totally lacked activity but was viable, showing that the enzyme is not essential for growth.
MeSH Terms
Acetylmuramyl-Alanyl-Isoglutamine/analogs & derivatives,metabolism
Amino Acid Sequence
Cell Wall/metabolism
Chromosome Mapping
Escherichia coli/enzymology,genetics,growth & development
Genes, Bacterial
Molecular Sequence Data
Mutation
Peptide Synthases/genetics
Peptidoglycan/metabolism
Recombinant Proteins/biosynthesis
Uridine Diphosphate N-Acetylmuramic Acid/metabolism
Chemicals
Peptidoglycan
Recombinant Proteins
Uridine Diphosphate N-Acetylmuramic Acid
Acetylmuramyl-Alanyl-Isoglutamine
muramylNAc-Ala-isoGln-Lys-tripeptide
Peptide Synthases
UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mengin-Lecreulx D
Unité de Recherche Associée 1131 du Centre National de la Recherche Scientifique, Université Paris-Sud, Orsay, France.
[email protected]
van Heijenoort J
Park J T
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