Information on EC 2.1.3.9 - N-acetylornithine carbamoyltransferase

Word Map on EC 2.1.3.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.1.3.9
-
RECOMMENDED NAME
GeneOntology No.
N-acetylornithine carbamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + N2-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl group transfer
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
-
-
L-arginine biosynthesis III (via N-acetyl-L-citrulline)
-
-
Metabolic pathways
-
-
arginine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase
Differs from EC 2.1.3.3, ornithine carbamoyltransferase. This enzyme replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of several Eubacteria and has no catalytic activity with L-ornithine as substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-69-8
cf EC 2.1.3.3
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas
metabolism
-
AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas
physiological function
-
arginine biosynthesis
additional information
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 + N2-acetyl-L-ornithine
phosphate + N-acetyl-L-citrulline
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
carbamoyl phosphate + N2-acetyl-L-ornithine
phosphate + N-acetyl-L-citrulline
show the reaction diagram
-
-
-
-
?
additional information
?
-
PDB
SCOP
CATH
ORGANISM
UNIPROT
Clostridium acetobutylicum (strain EA 2018)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure in presence and absence of N-acetylcitrulline
-
purified recombinant enzyme in binary complex with its substrates, carbamoyl phosphate or N-acetyl-L-ornithine, and in ternary complex with carbamoyl phosphate and N-acetyl-L-norvaline, hanging drop vapour diffusion method, preparation by mixing of 0.002 ml of 12 mg/ml protein solution with an equal volume of reservoir solution containing the ligands, cryoprotection, X-ray diffraction structure determination and analysis at 1.8-1.95 A resolution, modeling of the transition state complex
-
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K302A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
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
K302R
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
-
computer model of molecular dynamic
Show AA Sequence (268 entries)
Please use the Sequence Search for a specific query.