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Information on EC 2.1.3.3 - ornithine carbamoyltransferase and Organism(s) Campylobacter jejuni and UniProt Accession Q9PNU6

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EC Tree
IUBMB Comments
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.
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This record set is specific for:
Campylobacter jejuni
UNIPROT: Q9PNU6
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Word Map
The taxonomic range for the selected organisms is: Campylobacter jejuni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
oct, ornithine transcarbamylase, ornithine carbamoyltransferase, otcase, ornithine transcarbamoylase, carbamoyltransferase, ornithine carbamyl transferase, ornithine carbamyltransferase, catabolic ornithine carbamoyltransferase, anabolic ornithine carbamoyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
anabolic ornithine transcarbamoylase
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ornithine carbamoyltransferase
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carbamoyltransferase, ornithine
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carbamylphosphate-ornithine transcarbamylase
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citrulline phosphorylase
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L-ornithine carbamoyltransferase
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L-ornithine carbamyltransferase
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-
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L-ornithine transcarbamylase
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ornithine carbamyltransferase
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ornithine transcarbamoylase
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OTC
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:L-ornithine carbamoyltransferase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-69-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + L-ornithine
L-citrulline + phosphate
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. jejuni, gene argF
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
aOTC is a widespread enzyme that is found in a large variety of organisms from bacteria to mammals
metabolism
anabolic ornithine transcarbamoylase is involved in the urea cycle and L-arginine biosynthesis
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
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene argF, expression of His-tagged aOTC in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shabalin, I.G.; Porebski, P.J.; Cooper, D.R.; Grabowski, M.; Onopriyenko, O.; Grimshaw, S.; Savchenko, A.; Chruszcz, M.; Minor, W.
Structure of anabolic ornithine carbamoyltransferase from Campylobacter jejuni at 2.7 A resolution
Acta Crystallogr. Sect. F
68
1018-1024
2012
Campylobacter jejuni (Q9PNU6), Campylobacter jejuni, Campylobacter jejuni NCTC 11168 (Q9PNU6)
Manually annotated by BRENDA team