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Literature summary extracted from

  • Li, Y.; Yu, X.; Ho, J.; Fushman, D.; Allewell, N.M.; Tuchman, M.; Shi, D.
    Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase (2010), Biochemistry, 49, 6887-6895.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.9 recombinant expression of wild-type and mutant enzymes in Escherichia coli Xanthomonas campestris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.9 wild-type and mutant AOTCase complexed with bisubstrate analogue Ndelta-(phosphonoacetyl)-Nalpha-acetyl-L-ornithine, hanging drop vapor diffusion method, mixing of 0.002 ml 10 mg/ml protein in solution with 0.0016 ml of reservoir solution and 0.0004 ml 10 mM ligand solution. The reservoir solution contains 20% w/v PEG 3350, 0.2 M lithium sulfate, and 0.1 M Bis-Tris, pH 6.0, X-ray diffraction structure determination and analysis at 1.8-2.2 A resolution, molecular replacement Xanthomonas campestris

Protein Variants

EC Number Protein Variants Comment Organism
2.1.3.9 K302A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Xanthomonas campestris
2.1.3.9 K302E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The side-chain of Glu302 in the K302E mutant structure is well defined and anchored by hydrogen bonding interaction with the main-chain nitrogen atom of Arg298 and weakly hydrogen bonded to the main-chain nitrogen atom of Ser253 Xanthomonas campestris
2.1.3.9 K302R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Xanthomonas campestris

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.9 Xanthomonas campestris Q8P8J2
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.1.3.9 side-chain modification Lys302 is post-translationally carboxylated. The carboxyl group on Lys302 forms a strong hydrogen bonding network with surrounding active site residues, Lys252, Ser253, His293, and Glu92 from the adjacent subunit either directly or via a water molecule. The carboxyl group is involved in binding N-acetyl-L-ornithine via a water molecule Xanthomonas campestris

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.9 recombinant wild-type and mutant enzymes from Escherichia coli Xanthomonas campestris

Synonyms

EC Number Synonyms Comment Organism
2.1.3.9 AOTCase
-
 Xanthomonas campestris
2.1.3.9 N-acetyl-L-ornithine transcarbamylase
-
 Xanthomonas campestris

General Information

EC Number General Information Comment Organism
2.1.3.9 evolution AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas Xanthomonas campestris
2.1.3.9 metabolism AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas Xanthomonas campestris
2.1.3.9 additional information Lys302 is post-translationally carboxylated. The carboxyl group on Lys302 forms a strong hydrogen bonding network with surrounding active site residues, Lys252, Ser253, His293, and Glu92 from the adjacent subunit either directly or via a water molecule. The carboxyl group is involved in binding N-acetyl-L-ornithine via a water molecule. The posttranslational modification of lysine 302 has an important role in catalysis Xanthomonas campestris