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EC Number
Title
Organism
2.3.1.1
A novel UPLC-MS/MS based method to determine the activity of N-acetylglutamate synthase in liver tissue
Homo sapiens
2.3.1.1
Crystal structure of L-glutamate N-acetyltransferase ArgA from Mycobacterium tuberculosis
Mycobacterium tuberculosis
2.3.1.1
Crystal structure of L-glutamate N-acetyltransferase ArgA from Mycobacterium tuberculosis
Mycobacterium tuberculosis H37Rv
2.3.1.1
Effect of arginine on oligomerization and stability of N-acetylglutamate synthase
Xanthomonas campestris
2.3.1.1
Effect of arginine on oligomerization and stability of N-acetylglutamate synthase
Maricaulis maris
2.3.1.1
Effect of arginine on oligomerization and stability of N-acetylglutamate synthase
Mus musculus
2.3.1.1
Structural insights into the substrate binding mechanism of novel ArgA from Mycobacterium tuberculosis
Mycobacterium tuberculosis
2.3.1.1
Structural insights into the substrate binding mechanism of novel ArgA from Mycobacterium tuberculosis
Mycobacterium tuberculosis H37Rv
2.3.1.1
A modified assay system for enzymes involved in N-acetyl group transfer reactions: its use to study enzymes involved in ornithine biosynthesis in plants
Pisum sativum
2.3.1.1
A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis. Acetylglutamate synthase activity requires complex formation with acetylglutamate kinase
Saccharomyces cerevisiae
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