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UDP-N-acetylmuramate-L-alanine ligase activity

Known as: UDP-N-acetylmuramate:L-alanine ligase (ADP-forming), UDP-MurNAc:L-alanine ligase activity, UDPMurNAc-L-alanine synthetase activity 
Catalysis of the reaction: L-alanine + ATP + UDP-N-acetylmuramate = ADP + 2 H(+) + phosphate + UDP-N-acetylmuramoyl-L-alanine. [EC:6.3.2.8, RHEA… Expand
National Institutes of Health

Papers overview

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Highly Cited
2003
Highly Cited
2003
Functional and biochemical analysis of Chlamydia trachomatis MurC, an enzyme displaying UDP-N-acetylmuramate:amino acid ligase activity.
Chlamydiae are unusual obligate intracellular bacteria that cause serious infections in humans. Chlamydiae contain genes that… Expand
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Highly Cited
2002
Highly Cited
2002
Benzylidene rhodanines as novel inhibitors of UDP-N-acetylmuramate/L-alanine ligase.
Benzylidene rhodanines are novel inhibitors of UDP N-acetylmuramate/L-alanine ligase. They showed selective whole-cell activity… Expand
Highly Cited
2000
Highly Cited
2000
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… Expand
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Review
1998
Review
1998
Control of peptidoglycan synthesis in vancomycin-resistant enterococci: D,D-peptidases and D,D-carboxypeptidases
  • P. Reynolds
  • Cellular and Molecular Life Sciences CMLS
  • 1998
    • Corpus ID: 31941276
Abstract. Resistance to glycopeptide antibiotics in enterococci results from the synthesis of peptidoglycan precursors with low… Expand
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Highly Cited
1997
Highly Cited
1997
High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system.
Using the maltose-binding protein (MBP) fusion vector pMAL-c1 from C. V. Maina et al. (1988, Gene 74, 365-373), we have… Expand
Highly Cited
1997
Highly Cited
1997
Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase.
Initial velocity methods were used to probe the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L… Expand
Highly Cited
1996
Highly Cited
1996
Biochemical evidence for the formation of a covalent acyl-phosphate linkage between UDP-N-acetylmuramate and ATP in the Escherichia coli UDP-N-acetylmuramate:L-alanine ligase-catalyzed reaction.
In the peptidoglycan biosynthesis pathway in Escherichia coli, UDP-N-acetylmuramate:L-alanine ligase (MurC) catalyzes the… Expand
1996
1996
Structural studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase.
Uridine diphosphate N-acetylmuramate:L-alanine ligase (EC 6.3.2.8, UNAM:L-Ala ligase or MurC gene product) adds the first amino… Expand
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Highly Cited
1995
Highly Cited
1995
Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli.
The UDP-N-acetylmuramate:L-alanine ligase of Escherichia coli was over-produced in strains harbouring recombinant plasmids… Expand
1973
1973
Purification and properties of uridine diphosphate N-acetylmuramate: L-alanine ligase.
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