Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Shi, D.; Caldovic, L.; Jin, Z.; Yu, X.; Qu, Q.; Roth, L.; Morizono, H.; Hathout, Y.; Allewell, N.M.; Tuchman, M.
    Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase (2006), Acta Crystallogr. Sect. F, F62, 1218-1222.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.1 expression in Escherichia coli Xanthomonas campestris
2.7.2.8 expression in Escherichia coli, selenomethionine substituted enzyme, site directed mutagenesis Xanthomonas campestris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.1 sitting drop and hanging-drop vapor diffusion method, crystals belong to the hexagonal space group P6(2)22, with unit-cell parameters a = b = 134.60, c = 192.11 A, and diffract to about 3.0 A resolution Xanthomonas campestris
2.7.2.8 of the recombinant wild type protein, the selenomethionine substituted enzyme, the mutants and the methylated enzyme, cocrystallization with ATP, ADP, acetyl-CoA, CoA, N-acetyl-L-glutamate, adenylylimidodiphosphate, arginine Xanthomonas campestris

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.8 E186A/E387A to improve resolution in crystallization Xanthomonas campestris
2.7.2.8 E416A/K417A to improve resolution in crystallization Xanthomonas campestris
2.7.2.8 E94A/K95A to improve resolution in crystallization Xanthomonas campestris
2.7.2.8 K26A/E27A to improve resolution in crystallization Xanthomonas campestris
2.7.2.8 K279A/E280A to improve resolution in crystallization Xanthomonas campestris
2.7.2.8 K419A to improve resolution in crystallization Xanthomonas campestris

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.1 Xanthomonas campestris
-
-
-
2.7.2.8 Xanthomonas campestris Q8P8J6
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.2.8 side-chain modification methylation of surface lysine residues Xanthomonas campestris

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.1
-
 Xanthomonas campestris
2.7.2.8 of the recombinant protein Xanthomonas campestris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.8 acetyl-CoA + L-glutamate
-
 Xanthomonas campestris coenzyme A + N-acetyl-L-glutamate ancestral bifunctional N-acetylglutamate synthase and kinase ?
2.7.2.8 ATP + N-acetyl-L-glutamate
-
 Xanthomonas campestris ADP + N-acetyl-L-glutamate 5-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.1 N-acetylglutamate synthase/kinase bifunctional enzyme Xanthomonas campestris
2.7.2.8 acetylglutamate kinase
-
 Xanthomonas campestris
2.7.2.8 amino-acid acetyltransferase
-
 Xanthomonas campestris
2.7.2.8 N-acetylglutamate kinase
-
 Xanthomonas campestris
2.7.2.8 NagK
-
 Xanthomonas campestris
2.7.2.8 NAGS-K
-
 Xanthomonas campestris