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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
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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…
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National Institutes of Health
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2020
2020
Peptidoglycan Hydrolases RipA and Ami1 Are Critical for Replication and Persistence of Mycobacterium tuberculosis in the Host
C. Healy
,
Alexandre Gouzy
,
S. Ehrt
mBio
2020
Corpus ID: 212405065
Tuberculosis (TB) is a major global heath burden, with 1.6 million people succumbing to the disease every year. The search for…
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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
L. Hesse
,
J. Bostock
,
S. Dementin
,
D. Blanot
,
D. Mengin-Lecreulx
,
I. Chopra
Journal of bacteriology
2003
Corpus ID: 412976
ABSTRACT Chlamydiae are unusual obligate intracellular bacteria that cause serious infections in humans. Chlamydiae contain genes…
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Highly Cited
2000
Highly Cited
2000
Comparison of the UDP-N-Acetylmuramate:l-Alanine Ligase Enzymes from Mycobacterium tuberculosis andMycobacterium leprae
S. Mahapatra
,
D. Crick
,
P. Brennan
Journal of bacteriology
2000
Corpus ID: 955726
ABSTRACT In the peptidoglycan of Mycobacterium leprae,l-alanine of the side chain is replaced by glycine. When expressed in…
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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…
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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.
K. Pryor
,
B. Leiting
Protein expression and purification
1997
Corpus ID: 19994095
Using the maltose-binding protein (MBP) fusion vector pMAL-c1 from C. V. Maina et al. (1988, Gene 74, 365-373), we have…
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Highly Cited
1997
Highly Cited
1997
Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase.
J. J. Emanuele
,
H. Jin
,
J. Yanchunas
,
J. Villafranca
Biochemistry
1997
Corpus ID: 25020447
Initial velocity methods were used to probe the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L…
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1996
1996
Structural studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase.
H. Jin
,
J. J. Emanuele
,
+5 authors
J. Villafranca
Biochemistry
1996
Corpus ID: 32044478
Uridine diphosphate N-acetylmuramate:L-alanine ligase (EC 6.3.2.8, UNAM:L-Ala ligase or MurC gene product) adds the first amino…
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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.
P. Falk
,
K. M. Ervin
,
K. Volk
,
H. T. Ho
Biochemistry
1996
Corpus ID: 46703920
In the peptidoglycan biosynthesis pathway in Escherichia coli, UDP-N-acetylmuramate:L-alanine ligase (MurC) catalyzes the…
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1996
1996
Study of the overproduced uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli.
D. Liger
,
A. Masson
,
D. Blanot
,
J. van Heijenoort
,
C. Parquet
Microbial drug resistance
1996
Corpus ID: 35057411
The UDP-N-acetylmuramate:L-alanine ligase of Escherichia coli is responsible for the addition of the first amino acid of the…
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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.
D. Liger
,
A. Masson
,
D. Blanot
,
J. van Heijenoort
,
C. Parquet
European journal of biochemistry
1995
Corpus ID: 24753376
The UDP-N-acetylmuramate:L-alanine ligase of Escherichia coli was over-produced in strains harbouring recombinant plasmids…
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