Literature summary for 2.1.3.9 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.

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
K302A	site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme	Xanthomonas campestris
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
K302R	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	Xanthomonas campestris

Organism

Organism	UniProt	Comment	Textmining
Xanthomonas campestris	Q8P8J2	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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)

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

Synonyms

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

General Information

General Information	Comment	Organism
evolution	AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas	Xanthomonas campestris
metabolism	AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas	Xanthomonas campestris
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