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The Crystal Structure of N-Acetyl-L-glutamate Synthase from Neisseria gonorrhoeae Provides Insights into Mechanisms of Catalysis and Regulation*
The crystal structures of N-acetylglutamate synthase (NAGS) in the arginine biosynthetic pathway of Neisseria gonorrhoeae complexed with acetyl-CoA and with CoA plus N-acetylglutamate have been
Cloning and expression of the human N-acetylglutamate synthase gene.
A cDNA sequence containing the "conserved domain" complements an NAGS-deficient Escherichia coli strain and the recombinant protein has arginine-responsive NAGs catalytic activity.
Identification, cloning and expression of the mouse N-acetylglutamate synthase gene.
The mouse (Mus musculus) and human NAGS genes are identified using their similarity to the respective Neurospora crassa gene and the deduced amino acid sequence contains a putative mitochondrial targeting signal at the N-terminus.
Antioxidant activities of compounds isolated from Dalbergia odorifera T. Chen and their inhibition effects on the decrease of glutathione level of rat lens induced by UV irradiation
Abstract Four compounds were isolated from the root of Dalbergia odorifera T. Chen and identified by chemical and spectroscopic methods as 2′- O -methyl-isoliquiritigenin ( 1 ), odoriflavene ( 2 ),
Acetylornithine Transcarbamylase: a Novel Enzyme in Arginine Biosynthesis
A potent inhibitor, N(alpha)-acetyl-N(delta)-phosphonoacetyl -L-ornithine, was synthesized and showed a midpoint of inhibition at approximately 22 nM; this compound may prove to be a useful starting point for designing inhibitors specific to this novel family of transcarbamylases.
Crystal structure of a transcarbamylase-like protein from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution.
The three-dimensional structure and the fact that this protein is essential for arginine biosynthesis in the anaerobic bacterium Bacteroides fragilis suggest strongly that it is a new member of the transcarbamylase family.
Crystal Structure of N-Acetylornithine Transcarbamylase from Xanthomonas campestris
This novel protein structure provides a starting point for rational design of specific analogs that may be useful in combating human and plant pathogens that utilize acetylornithine transcarbamylase rather than ornithinetranscarbamymylase.
A Novel N-Acetylglutamate Synthase Architecture Revealed by the Crystal Structure of the Bifunctional Enzyme from Maricaulis maris
Structures and sequence comparisons suggest that the linker residue 291 may determine whether arginine acts as an allosteric inhibitor or activator in homologous enzymes in microorganisms and vertebrates.
Structure and Catalytic Mechanism of a Novel N-Succinyl-l-ornithine Transcarbamylase in Arginine Biosynthesis of Bacteroides fragilis*
Comparison of the structures of the new protein with those recently reported for N-acetyl-l-ornithine transcarbamylase indicates that amino acid residue 90 (B. fragilis numbering) plays an important role in conferring substrate specificity in N-succinyl- l-ORNithine versus N-ordithine.
Structures of N‐acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis
Crystal structures of the binary complexes of AOTCase with its substrates, carbamoyl phosphate or N‐acetyl‐L‐ornithine (AORN), and the ternary complexes provide insight into the mode of substrate binding and the mechanism of the transcarbamoylation reaction.