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
2.3.1.35
-
RECOMMENDED NAME
GeneOntology No.
glutamate N-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
substrate binding structure, oxyanion stabilization mechanism of the enzyme-substrate complex, the ping pong reaction mechanism involves Gly112 and Thr181, active site structure
P0DJQ5
N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
residue T181 becomes acetylated and 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 which 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
P0DJQ5
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
arginine metabolism
-
-
Biosynthesis of antibiotics
-
-
L-arginine biosynthesis II (acetyl cycle)
-
-
Metabolic pathways
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylglutamate synthetase
-
-
-
-
acetylglutamate-acetylornithine transacetylase
-
-
-
-
acetylglutamic synthetase
-
-
-
-
acetylglutamic-acetylornithine transacetylase
-
-
-
-
acetylornithinase
-
-
-
-
acetylornithine glutamate acetyltransferase
-
-
-
-
acetyltransferase, glutamate
-
-
-
-
alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase
-
-
-
-
glutamate acetyltransferase
-
-
-
-
N-acetyl-L-glutamate synthetase
-
-
-
-
ornithine acetyltransferase
-
-
-
-
ornithine transacetylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37257-14-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
no activity in Sulfolobus solfataricus
-
-
-
Manually annotated by BRENDA team
isoform OAT2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
C1KGU6
overexpression of a OTase in Corynebacterium crenatum leads to an improvement of L-Arginine production
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-glutamate
CoA + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + H2O
L-ornithine + acetate
show the reaction diagram
-
hydrolytic activity is 1% of the transferase activity
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
-
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
P0DJQ5
-
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
C1KGU6
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
specific for L-glutamate
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
specific for L-glutamate and L-ornithine, first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
P0DJQ5
step in clavulanic acid biosynthesis via formation of arginine
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
CLGAT can effectively participate in the biosynthesis of citrulline in leaves of during drought/strong-light stress
-
-
?
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
-
-
-
-
?
L-ornithine + N-acetyl-L-glutamate
N2-acetyl-L-ornithine + L-glutamate
show the reaction diagram
P0DJQ5
-
-
-
?
additional information
?
-
P0DJQ5
enzyme also shows low hydrolase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
-
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
first step in arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
bifunctional enzyme catalyzes also the fifth step of arginine biosynthesis
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
P0DJQ5
step in clavulanic acid biosynthesis via formation of arginine
-
-
r
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
show the reaction diagram
-
CLGAT can effectively participate in the biosynthesis of citrulline in leaves of during drought/strong-light stress
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no specific cofactor
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Methylornithine
-
-
N-Bromoacetylornithine
-
-
p-chloromercuribenzoate
-
-
additional information
-
not: iodoacetate
-
additional information
-
not inhibited by citrulline or arginine at physiologically relevant high concentrations
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-arginine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
alpha-N-acetyl-L-ornithine
-
-
0.4
alpha-N-acetyl-L-ornithine
-
-
1
alpha-N-acetyl-L-ornithine
-
-
2.7
alpha-N-acetyl-L-ornithine
-
-
3.6
alpha-N-acetyl-L-ornithine
-
-
5.5
alpha-N-acetyl-L-ornithine
-
-
6.25
alpha-N-acetyl-L-ornithine
-
-
8.1
alpha-N-acetyl-L-ornithine
-
-
9.6
alpha-N-acetyl-L-ornithine
-
-
0.13
L-glutamate
-
-
7.2
L-glutamate
-
-
11.3
L-glutamate
-
-
14.65
L-glutamate
-
-
17.8
L-glutamate
-
pH 7.0
19.2
L-glutamate
-
-
27.9
L-glutamate
-
-
1.5
L-ornithine
-
-
17.1
N-acetylglutamate
-
-
3.4
N2-Acetyl-L-ornithine
-
pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.2
-
mutant G362S; mutant G362S, presence of 1 mM L-arginine
3.4
-
mutant G286P, presence of 1 mM L-arginine
3.5
-
mutant G286P
4.3
-
mutant F35C, presence of 1 mM L-arginine
9.7
-
mutant F35C
12.2
-
mutant F121C
12.3
-
wild-type; wild-type, presence of 1 mM L-arginine
12.6
-
mutant G360P, presence of 1 mM L-arginine
13
-
mutant G360P
13.1
-
mutant E354A, presence of 1 mM L-arginine
15.3
-
mutant F121C, presence of 1 mM L-arginine
15.5
-
mutant E354A
26.7
-
mutant E280A, presence of 1 mM L-arginine
26.9
-
mutant E280A
42.6
-
mutant G288S, presence of 1 mM L-arginine
46
-
mutant G288S
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
C1KGU6
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 80
-
40C: about 40% of maximal activity, 80C: about 45% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39700
C1KGU6
calculated from cDNA
718612
57000
-
gel filtration
486801
83000
-
gel filtration
486800
90000
-
gel filtration
673532
110000
-
gel filtration
486804
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 41000, calculated
?
-
x * 41000, calculated
-
heterodimer
-
alphabeta, 1 * 31000 + 1 * 26000, SDS-PAGE
heterodimer
C1KGU6
alpha- and beta-subunits can not self-assemble to active OATase conformation
tetramer
P0DJQ5
alpha2beta2 structure, the interface partly defines the active site
tetramer
-
2 * 21300 + 2 * 23500, calculated from sequence
heterotetramer
-
alpha2beta2, 2 * 19000 + 2 * 25000, SDS-PAGE
additional information
P0DJQ5
2 domain structure, the larger domain consists of an alphabetabetaalpha sandwich typical for N-terminal nucleophile Ntn enzymes
additional information
-
the domain 1 of the enzyme has a socalled DOM-fold, which is a structure with crossing loops with a two-layered beta/alpha architecture of particular topology, also found in the L-aminopeptidase D-Ala-esterase/amidase and the molybdenum cofactor-binding domain, structure-function relationship, comparison of sequence basis for the structure by multiple amino acid sequence alignment, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the two subunits withj molecular masses of 21300 Da and 23500 Da are derived from a single precursor polypeptide, suggesting that the CLGAT precursor is cleaved autocatalytically at the conserved ATML motif. The first 26-amino acid sequence at the N-terminus of the precursor functions as a chloroplast transit peptide
proteolytic modification
P0DJQ5
enzyme belongs to the N-terminal nucleophile hydrolase class of self-processing acetyltransferases
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.
-
diffraction to 1.7 A resolution, space group P212121
-
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
-
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
P0DJQ5
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)
P0DJQ5
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
P0DJQ5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
inactivation after 20 min
486804
70
-
stable up to
673532
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
-
glutamate decreases stability
-
N-acetylglutamate stabilizes and protects against inactivating effect of heat and 4 M urea
-
N2-acetylornithine stabilizes
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 30% loss of activity after storage overnight
-
-20C, 10% loss activity per week
-
4C, 10% loss activity per week
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
C1KGU6
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli and yeast arg2
-
overexpression in Escherichia coli
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E354A
-
change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
F121C
-
change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
G360P
-
change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
G362S
-
change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
D150G
P0DJQ5
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
P0DJQ5
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
P0DJQ5
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
P0DJQ5
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
P0DJQ5
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
P0DJQ5
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
-
change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
F35C
-
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
-
change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
G288S
-
change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine inhibition and decreases synthase activity