EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.3.3 | gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL | Campylobacter jejuni |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.3.3 | unliganded aOTC, hanging drop vapor diffusion method, mixing of 500 nl 10 mg/ml protein solution with 500 nl well solution containing 25% PEG 3350, 0.2 M NaCl, 0.1 M HEPES, pH 8.0, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement and modeling | Campylobacter jejuni |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.3 | carbamoyl phosphate + L-ornithine | Campylobacter jejuni | - |
L-citrulline + phosphate | - |
? | |
2.1.3.3 | carbamoyl phosphate + L-ornithine | Campylobacter jejuni NCTC 11168 | - |
L-citrulline + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.3.3 | Campylobacter jejuni | Q9PNU6 | subsp. jejuni, gene argF | - |
2.1.3.3 | Campylobacter jejuni NCTC 11168 | Q9PNU6 | subsp. jejuni, gene argF | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.3.3 | gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL | Campylobacter jejuni |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.3 | carbamoyl phosphate + L-ornithine | - |
Campylobacter jejuni | L-citrulline + phosphate | - |
? | |
2.1.3.3 | carbamoyl phosphate + L-ornithine | the mechanism of the aOTC-catalyzed reaction involves nucleophilic attack of the electron pair of the epsilon-amino group of L-ornithine on the carbonyl group of carbamoyl phosphate | Campylobacter jejuni | L-citrulline + phosphate | - |
? | |
2.1.3.3 | carbamoyl phosphate + L-ornithine | - |
Campylobacter jejuni NCTC 11168 | L-citrulline + phosphate | - |
? | |
2.1.3.3 | carbamoyl phosphate + L-ornithine | the mechanism of the aOTC-catalyzed reaction involves nucleophilic attack of the electron pair of the epsilon-amino group of L-ornithine on the carbonyl group of carbamoyl phosphate | Campylobacter jejuni NCTC 11168 | L-citrulline + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.3.3 | trimer | forms a head-to-head pseudohexamer in the asymmetric unit, each monomer is composed of an N-terminal CP-binding domain and a C-terminal ORN-binding domain joined by two interdomain helices. Conformation of the B2-H3 loop, residues 68-78, is involved in binding CP in an adjacent subunit of the trimer, overview | Campylobacter jejuni |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.3.3 | anabolic ornithine transcarbamoylase | - |
Campylobacter jejuni |
2.1.3.3 | AOTC | - |
Campylobacter jejuni |
2.1.3.3 | ornithine carbamoyltransferase | - |
Campylobacter jejuni |
2.1.3.3 | OTC | - |
Campylobacter jejuni |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.3.3 | evolution | aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals | Campylobacter jejuni |
2.1.3.3 | metabolism | anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis | Campylobacter jejuni |
2.1.3.3 | additional information | the conserved active site of Campylobacter jejuni aOTC consists of residues from both carbamoyl phosphate binding and L-ornithine-binding domains of the subunit and the B2-H3 loop, residues 68-78, from an adjacent subunit of the trimer, active site structure, overview | Campylobacter jejuni |
2.1.3.3 | physiological function | OTC catalyzes the reversible transfer of the carbamoyl group from carbamoyl phosphate to the Nepsilon atom of L-ornithine to produce L-citrulline. There are two types of enzyme: anabolic, aOTC, and catabolic, cOTC. Anabolic OTCs catalyze the forward reaction and participate in the urea cycle and L-arginine biosynthesis | Campylobacter jejuni |