Comparison of the UDP-N-acetylmuramate:L-alanine ligase enzymes from Mycobacterium tuberculosis and Mycobacterium leprae.
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.
Mahapatra
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Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1677, USA.
Crick
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DC
Brennan
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D000409:Alanine / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005798:Genes, Bacterial; D005998:Glycine / Q000378:metabolism*; D008969:Molecular Sequence Data; D005810:Multigene Family; D009166:Mycobacterium leprae / Q000201:enzymology* / Q000235:genetics; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics; D010453:Peptide Synthases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014166:Transferases; D017855:Transferases (Other Substituted Phosphate Groups)
D001426:Bacterial Proteins; D014166:Transferases; D017855:Transferases (Other Substituted Phosphate Groups); C079803:mraY protein, Bacteria; D010453:Peptide Synthases; C023229:UDP-N-acetylmuramoyl-alanine synthetase; D000409:Alanine; D005998:Glycine