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 ACCESSION NO.
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
Q53940
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
Q53940
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
arginine biosynthesis II (acetyl cycle)
-
Biosynthesis of secondary metabolites
-
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 ACCESSION NO.
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
-
-
-
-
argJ
C1KGU6
gene name
glutamate acetyltransferase
-
-
-
-
N-acetyl-L-glutamate synthetase
-
-
-
-
ornithine acetyl transferase
P0DJQ5
-
ornithine acetyltransferase
-
-
-
-
ornithine acetyltransferase
C1KGU6
-
ornithine acetyltransferase
-
-
ornithine transacetylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37257-14-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
gene orf6
Q53940
UniProt
Manually annotated by BRENDA team
isoform OAT2
Q53940
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
Q53940
-
-
-
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
Q53940
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
?
-
Q53940
enzyme also shows low hydrolase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
Q53940
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no specific cofactor
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
L-arginine
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
14.65
-
L-glutamate
-
-
17.8
-
L-glutamate
-
pH 7.0
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
4.7
-
-
above
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
71
-
-
wild-type
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
C1KGU6, -
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
C1KGU6, -
assay at
37
-
-
assay at
95
-
-
more than 95C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
80
-
40C: about 40% of maximal activity, 80C: about 45% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
39700
-
C1KGU6, -
calculated from cDNA
57000
-
-
gel filtration
83000
-
-
gel filtration
90000
-
-
gel filtration
110000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
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
heterotetramer
-
alpha2beta2, 2 * 19000 + 2 * 25000, SDS-PAGE
tetramer
Q53940
alpha2beta2 structure, the interface partly defines the active site
tetramer
-
2 * 21300 + 2 * 23500, calculated from sequence
additional information
Q53940
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 ACCESSION NO.
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
Q53940
enzyme belongs to the N-terminal nucleophile hydrolase class of self-processing acetyltransferases
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q53940
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
Q53940
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
-
inactivation after 20 min
70
-
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, 30% loss of activity after storage overnight
-
-20C, 10% loss activity per week
-
4C, 10% loss activity per week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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