Information on EC 2.3.1.35 - glutamate N-acetyltransferase

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

EC NUMBER
COMMENTARY hide
2.3.1.35
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RECOMMENDED NAME
GeneOntology No.
glutamate N-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
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arginine metabolism
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Biosynthesis of antibiotics
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L-arginine biosynthesis II (acetyl cycle)
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase
Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-14-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
functional study reveals that OATase from Corynebacterium crenatum SYPA5-5 is a bifunctional enzyme with the functions of acetylglutamate synthase and acetylornithine deacetylase
UniProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Sulfolobus solfataricus
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
overexpression of a OTase in Corynebacterium crenatum leads to an improvement of L-Arginine production
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
show the reaction diagram
L-ornithine + N-acetyl-L-glutamate
N2-acetyl-L-ornithine + L-glutamate
show the reaction diagram
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-
-
?
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
N2-butyryl-L-ornithine + H2O
L-ornithine + butyric acid
show the reaction diagram
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-
-
-
?
N2-propionyl-L-ornithine + glutamate
L-ornithine + N-propionylglutamate
show the reaction diagram
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-
-
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?
additional information
?
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enzyme also shows low hydrolase activity
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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
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no specific cofactor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Methylornithine
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L-ornithine
N-Bromoacetylornithine
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p-chloromercuribenzoate
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additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-arginine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 9.6
alpha-N-acetyl-L-ornithine
0.13 - 27.9
L-glutamate
1.5
L-ornithine
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17.1
N-acetylglutamate
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3.4
N2-Acetyl-L-ornithine
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pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2
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mutant G362S; mutant G362S, presence of 1 mM L-arginine
3.4
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mutant G286P, presence of 1 mM L-arginine
3.5
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mutant G286P
4.3
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mutant F35C, presence of 1 mM L-arginine
9.7
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mutant F35C
12.2
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mutant F121C
12.3
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wild-type; wild-type, presence of 1 mM L-arginine
12.6
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mutant G360P, presence of 1 mM L-arginine
13
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mutant G360P
13.1
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mutant E354A, presence of 1 mM L-arginine
15.3
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mutant F121C, presence of 1 mM L-arginine
15.5
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mutant E354A
26.7
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mutant E280A, presence of 1 mM L-arginine
26.9
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mutant E280A
42.6
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mutant G288S, presence of 1 mM L-arginine
46
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mutant G288S
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 80
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40C: about 40% of maximal activity, 80C: about 45% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39700
calculated from cDNA
57000
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gel filtration
83000
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gel filtration
90000
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gel filtration
110000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotetramer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of Mtb OAT in native form and in its complex with ornithine has been determined at 1.7 and 2.4 A resolutions, respectively. Ornithine binding does not alter the structure of Mtb OAT globally. Its presence stabilizes the three C-terminal residues that are disordered and not observed in the native structure. Stabilization of the C-terminal residues by ornithine reduces the size of the active-site pocket volume in the structure of the ORN complex. The interactions of ORN and the protein residues of Mtb OAT unambiguously delineate the active-site residues of this enzyme in Mtb.
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diffraction to 1.7 A resolution, space group P212121
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crystals grown by either the batch or hanging-drop vapour-diffusion method. The crystals belong to space group P4, with unit-cell parameters a = b = 66.98, c = 427.09 A. The use of the counterdiffusion technique is critical for the production of well ordered crystals
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crystallization of OAT2 in the presence of N-alpha-acetyl-L-glutamate leads to a structure in which residue T181 is acetylated, the carbonyl oxygen of the acyl-enzyme complex is located in an oxyanion hole and positioned to hydrogen bond with the backbone amide-NH of G112 and the alcohol of T111. Presence of two distinct acyl-enzyme complex structures. The two acyl-enzyme complex structures can interconvert by movement of the T111 side-chain alcohol hydrogen away from the oxyanion hole to hydrogen bond with the backbone carbonyl of the acylated residue, T181
crystals of OAT2 in complex with L-Glu are generated. Optimization of crystallization conditions lead to a 2.7 A resolution structure for OAT2 acylated at Thr-181 and in complex with L-Glu (referred to as the acetyl-OAT2-glutamate complex)
purified recombinant native and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, 12 mg/ml protein in 1.1-1.3 M ammonium sulfate, 0.04 M ammonium phosphate, 0.1 M Tris-HCl, pH 8.0, and 5-8% v/v glycerol, and in case of SeMet-enzyme 5 mM DTT, cryoprotection by 25% glycerol and 2.0 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.8 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
complete inactivation after dialysis against distilled water or 10 mM phosphate buffer, pH 7.5, for 16 h at 0C
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glutamate decreases stability
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N-acetylglutamate stabilizes and protects against inactivating effect of heat and 4 M urea
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N2-acetylornithine stabilizes
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
insensitive to O2
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10% loss activity per week
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0C, 30% loss of activity after storage overnight
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4C, 10% loss activity per week
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli and yeast arg2
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overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E354A
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change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
F121C
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change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
G360P
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change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
G362S
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change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
D150G
autoprocessing to alpha-,beta-subunits: 50% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 50% (wild-type 100%)
DELTA1389
autoprocessing to alpha-,beta-subunits: 100% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 40% (wild-type 100%)
E260A
autoprocessing to alpha-,beta-subunits: not determined (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 40% (wild-type 100%)
K170A
autoprocessing to alpha-,beta-subunits: 0% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 5% (wild-type 100%)
T148A
autoprocessing to alpha-,beta-subunits: 0% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 2% (wild-type: 100%)
T149A
autoprocessing to alpha-,beta-subunits: 80% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 10% (wild-type: 100%)
E280A
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change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
F35C
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change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation leads to partial inhibition of both synthase and kinase activities by arginine and decrease in synthase activity
G286P
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change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
G288S
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change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine inhibition and decreases synthase activity
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