Comparison of the UDP-N-acetylmuramate:L-alanine ligase enzymes from Mycobacterium tuberculosis and Mycobacterium leprae

J Bacteriol. 2000 Dec;182(23):6827-30. doi: 10.1128/JB.182.23.6827-6830.2000.

Abstract

In the peptidoglycan of Mycobacterium leprae, L-alanine of the side chain is replaced by glycine. When expressed in Escherichia coli, MurC (UDP-N-acetyl-muramate:L-alanine ligase) of M. leprae showed K(m) and V(max) for L-alanine and glycine similar to those of Mycobacterium tuberculosis MurC, suggesting that another explanation should be sought for the presence of glycine.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alanine / metabolism*
  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Gene Expression
  • Genes, Bacterial
  • Glycine / metabolism*
  • Molecular Sequence Data
  • Multigene Family
  • Mycobacterium leprae / enzymology*
  • Mycobacterium leprae / genetics
  • Mycobacterium tuberculosis / enzymology*
  • Mycobacterium tuberculosis / genetics
  • Peptide Synthases / genetics
  • Peptide Synthases / isolation & purification
  • Peptide Synthases / metabolism*
  • Sequence Homology, Amino Acid
  • Transferases (Other Substituted Phosphate Groups)
  • Transferases*

Substances

  • Bacterial Proteins
  • Transferases
  • Transferases (Other Substituted Phosphate Groups)
  • mraY protein, Bacteria
  • Peptide Synthases
  • UDP-N-acetylmuramoyl-alanine synthetase
  • Alanine
  • Glycine