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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… 
National Institutes of Health

Papers overview

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2020
2020
Peptidoglycan Hydrolases RipA and Ami1 Are Critical for Replication and Persistence of Mycobacterium tuberculosis in the Host
Tuberculosis (TB) is a major global heath burden, with 1.6 million people succumbing to the disease every year. The search for… 
Highly Cited
2003
Highly Cited
2003
Functional and Biochemical Analysis of Chlamydia trachomatis MurC, an Enzyme Displaying UDP-N-Acetylmuramate:Amino Acid Ligase Activity
ABSTRACT Chlamydiae are unusual obligate intracellular bacteria that cause serious infections in humans. Chlamydiae contain genes… 
Highly Cited
2000
Highly Cited
2000
Comparison of the UDP-N-Acetylmuramate:l-Alanine Ligase Enzymes from Mycobacterium tuberculosis andMycobacterium leprae
ABSTRACT In the peptidoglycan of Mycobacterium leprae,l-alanine of the side chain is replaced by glycine. When expressed in… 
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… 
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… 
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… 
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… 
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… 
1996
1996
Study of the overproduced uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli.
The UDP-N-acetylmuramate:L-alanine ligase of Escherichia coli is responsible for the addition of the first amino acid of the… 
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… 
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