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
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alanine / metabolism*
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Amino Acid Sequence
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Bacterial Proteins / genetics
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Cloning, Molecular
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Escherichia coli / genetics
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Gene Expression
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Genes, Bacterial
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Glycine / metabolism*
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Molecular Sequence Data
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Multigene Family
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Mycobacterium leprae / enzymology*
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Mycobacterium leprae / genetics
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Mycobacterium tuberculosis / enzymology*
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Mycobacterium tuberculosis / genetics
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Peptide Synthases / genetics
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Peptide Synthases / isolation & purification
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Peptide Synthases / metabolism*
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Sequence Homology, Amino Acid
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Transferases (Other Substituted Phosphate Groups)
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Transferases*
Substances
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Bacterial Proteins
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Transferases
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Transferases (Other Substituted Phosphate Groups)
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mraY protein, Bacteria
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Peptide Synthases
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UDP-N-acetylmuramoyl-alanine synthetase
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Alanine
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Glycine