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Information on EC 2.3.1.35 - glutamate N-acetyltransferase and Organism(s) Corynebacterium glutamicum and UniProt Accession Q59280
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2.3.1.35 glutamate N-acetyltransferaseIUBMB Comments
Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
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Word Map
- 2.3.1.35
- n-acetylglutamate
- n-acetylornithine
- gonorrhoeae
- clavuligerus
-
transacetylation
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clavulanic
- acetylornithinase
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2.3.1.1
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chorioretinal
- mango
-
gene-enzyme
- drug development
The taxonomic range for the selected organisms is: Corynebacterium glutamicum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ornithine acetyltransferase, oatase, clgat, glutamate acetyltransferase, glutamate n-acetyltransferase, mtb oat, n2-acetyl-l-ornithine:l-glutamate n-acetyltransferase, ornithine acetyl transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglutamate synthetase
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acetylglutamate-acetylornithine transacetylase
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-
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acetylglutamic synthetase
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acetylglutamic-acetylornithine transacetylase
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acetylornithinase
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acetylornithine glutamate acetyltransferase
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acetyltransferase, glutamate
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alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase
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glutamate acetyltransferase
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N-acetyl-L-glutamate synthetase
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ornithine acetyltransferase
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ornithine transacetylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
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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
37257-14-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
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-
-
-
?
N2-acetyl-L-ornithine + L-glutamate
L-ornithine + N-acetyl-L-glutamate
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-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-ornithine
feedback repression of L-ornithine synthesis, inhibition of OATase activity
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.004
enzyme activity in argJ-overexpressing strain 1006, pH 7.5, 30°C
0.008
enzyme activity in mutant strain 1006DELTAargR, pH 7.5, 30°C
0.015
enzyme activity in mutant strain 1006DELTAargR-DELTAargJ, pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
metabolism
physiological function
L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and L-glutamate as substrates. ArgJ recycles the acetyl group from acetylornithine. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035
metabolism
ArgJ plays a vital role in the L-citrulline biosynthesis. The enzyme exerts feedback inhibition on N-acetylglutamate synthase, pathway overview
metabolism
enzyme ArgJ strongly influences the production of L-ornithine in Corynebacterium glutamicum. L-Ornithine is a nonessential amino acid that is effective in treating liver diseases and in liver protection and wound healing and is capable of strengthening the heart. L-Ornithine is also an important constituent of the urea cycle. As the precursor of L-citrulline and L-arginine, L-ornithine is biosynthesized by the cyclic pathway in five steps through a series of acetylated intermediates in Corynebacterium glutamicum. In the ornithine biosynthetic pathway of Corynebacterium glutamicum, L-ornithine and N-acetylglutamate are produced by ornithine acetyltransferase (OATase, ArgJ) using acetylornithine and glutamate as substrates. Corynebacterium glutamicum possesses a monofunctional ArgJ protein that only exhibits OAT activity, lacks N-acetylglutamate synthetase activity, and only catalyses the fifth step of the L-citrulline biosynthesis pathway, in which glutamate is acetylated by the N-acetylglutamate synthase Cg3035. Inactivating ArgR decreases the feedback repression of L-ornithine synthesis and enhanced L-ornithine production in Corynebacterium glutamicum. Significant increase in L-ornithine concentration under homologous argJ overexpression
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
additional information
-
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
additional information
L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
additional information
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L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
additional information
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene argJ, cloning in Escherichia coli strain DH5alpha, recombinant overexpression in Corynebacterium glutamicum strain 1006
gene argJ, fnctional recombinant expression in Corynebacterium glutamicum mutant strain 1006DELTAargR-argJ, significant increase in L-ornithine concentration under homologous argJ overexpression
gene argJ, recombinant overexpression in Corynebacterium glutamicum strain ATCC 13032
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Shen, P.; Yan, M.; Li, Y.; Xu, L.
Implication of ornithine acetyltransferase activity on L-ornithine production in Corynebacterium glutamicum
Biotechnol. Appl. Biochem.
63
15-21
2016
Corynebacterium glutamicum (Q59280), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q59280)
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Yan, M.; Li, Y.; Guo, K.; Xu, L.
Improvement of L-citrulline production in Corynebacterium glutamicum by ornithine acetyltransferase
J. Ind. Microbiol. Biotechnol.
42
307-313
2015
Corynebacterium glutamicum (Q59280), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q59280), Corynebacterium glutamicum ATCC 13032
Hao, N.; Mu, J.; Hu, N.; Xu, S.; Shen, P.; Yan, M.; Li, Y.; Xu, L.
Implication of ornithine acetyltransferase activity on L-ornithine production in Corynebacterium glutamicum
Biotechnol. Appl. Biochem.
63
15-21
2016
Corynebacterium glutamicum (Q59280), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q59280), Corynebacterium glutamicum DSM 20300 (Q59280), Corynebacterium glutamicum JCM 1318 (Q59280), Corynebacterium glutamicum LMG 3730 (Q59280), Corynebacterium glutamicum NCIMB 10025 (Q59280)
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Release 2023.1 (January 2023)
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