The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively.
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
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
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
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
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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