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Literature summary for 2.3.1.35 extracted from

  • 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 (2016), Biotechnol. Appl. Biochem., 63, 15-21 .
    View publication on PubMed
Search for more literature for 2.3.1.35

Cloned(Commentary)

Cloned (Comment) Organism
gene argJ, fnctional recombinant expression in Corynebacterium glutamicum mutant strain 1006DELTAargR-argJ, significant increase in L-ornithine concentration under homologous argJ overexpression Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
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 Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
L-ornithine feedback repression of L-ornithine synthesis, inhibition of OATase activity Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum LMG 3730
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum ATCC 13032
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum JCM 1318
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum NCIMB 10025
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum DSM 20300
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q59280
-
-
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
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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) Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum LMG 3730 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum ATCC 13032 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum JCM 1318 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum NCIMB 10025 L-ornithine + N-acetyl-L-glutamate
-
 ?
N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum DSM 20300 L-ornithine + N-acetyl-L-glutamate
-
 ?

Synonyms

Synonyms Comment Organism
argJ
-
 Corynebacterium glutamicum
OATase
-
 Corynebacterium glutamicum
ornithine acetyltransferase
-
 Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Corynebacterium glutamicum

General Information

General Information Comment Organism
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) Corynebacterium glutamicum
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 Corynebacterium glutamicum
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 Corynebacterium glutamicum