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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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
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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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arginine metabolism
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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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-
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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
gene argJ
UniProt
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
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
-
-
-
?
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
-
-
-
-
?
N2-propionyl-L-ornithine + glutamate
L-ornithine + N-propionylglutamate
show the reaction diagram
-
-
-
-
?
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
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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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
L-citrulline
Corynebacterium glutamicum
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pH 7.5, 37°C
5
L-ornithine
Corynebacterium glutamicum
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pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
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enzyme activity in argJ-overexpressing strain 1006, pH 7.5, 30°C
0.008
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enzyme activity in mutant strain 1006DELTAargR, pH 7.5, 30°C
0.015
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enzyme activity in mutant strain 1006DELTAargR-DELTAargJ, pH 7.5, 30°C
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
95
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more than 95°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 80
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40°C: about 40% of maximal activity, 80°C: 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
19000
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alpha2beta2, 2 * 19000 + 2 * 25000, SDS-PAGE
21300
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2 * 21300 + 2 * 23500, calculated from sequence
23500
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2 * 21300 + 2 * 23500, calculated from sequence
25000
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alpha2beta2, 2 * 19000 + 2 * 25000, SDS-PAGE
26000
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alphabeta, 1 * 31000 + 1 * 26000, SDS-PAGE
31000
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alphabeta, 1 * 31000 + 1 * 26000, SDS-PAGE
39700
calculated from cDNA
41000
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x * 41000, calculated
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 0°C
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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
-20°C, 10% loss activity per week
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0°C, 30% loss of activity after storage overnight
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4°C, 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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gene argJ, cloning in Escherichia coli strain DH5alpha, recombinant overexpression in Corynebacterium glutamicum strain 1006
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gene argJ, recombinant overexpression in Corynebacterium glutamicum strain ATCC 13032
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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%)
DELTA1–389
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
additional information
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