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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.35 gene argJ, fnctional recombinant expression in Corynebacterium glutamicum mutant strain 1006DELTAargR-argJ, significant increase in L-ornithine concentration under homologous argJ overexpression Corynebacterium glutamicum
2.6.1.13 recombinant expression of wild-type and mutant enzymes in Corynebacterium glutamincum strain 1006, subcloning in Escherichia coli strain DH5alpha Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.35 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
2.6.1.13 additional information Corynebacterium glutamicum strain 1006 is engineered to overproduce L-ornithine as a major product by inactivating regulatory repressor argR gene and overexpressing argJ gene. A genome sequence analysis indicates that the argF gene encoding ornithine carbamoyltransferase in strain 1006 is mutated, resulting in the accumulation of a certain amount of L-ornithine (20.5 g/l). The OAT activity of Corynebacterium glutamicum mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006, showing a very high conversion ratio of sugar to acid (0.396 g/g) Corynebacterium glutamicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.35 L-ornithine feedback repression of L-ornithine synthesis, inhibition of OATase activity Corynebacterium glutamicum
2.6.1.13 L-ornithine substrate inhibition Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum LMG 3730
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum ATCC 13032
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum JCM 1318
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum NCIMB 10025
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium glutamicum DSM 20300
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.6.1.13 L-ornithine + 2-oxoglutarate Corynebacterium glutamicum
-
 L-glutamate 5-semialdehyde + L-glutamate
-
 r
2.6.1.13 L-ornithine + 2-oxoglutarate Corynebacterium glutamicum 1006
-
 L-glutamate 5-semialdehyde + L-glutamate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.3 no activity in Corynebacterium glutamicum 1006
-
-
-
2.3.1.35 Corynebacterium glutamicum Q59280
-
-
2.3.1.35 Corynebacterium glutamicum ATCC 13032 Q59280
-
-
2.3.1.35 Corynebacterium glutamicum DSM 20300 Q59280
-
-
2.3.1.35 Corynebacterium glutamicum JCM 1318 Q59280
-
-
2.3.1.35 Corynebacterium glutamicum LMG 3730 Q59280
-
-
2.3.1.35 Corynebacterium glutamicum NCIMB 10025 Q59280
-
-
2.6.1.13 Corynebacterium glutamicum
-
-
-
2.6.1.13 Corynebacterium glutamicum 1006
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.35 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum LMG 3730 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum ATCC 13032 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum JCM 1318 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum NCIMB 10025 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium glutamicum DSM 20300 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.6.1.13 L-ornithine + 2-oxoglutarate
-
 Corynebacterium glutamicum L-glutamate 5-semialdehyde + L-glutamate
-
 r
2.6.1.13 L-ornithine + 2-oxoglutarate
-
 Corynebacterium glutamicum 1006 L-glutamate 5-semialdehyde + L-glutamate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.35 argJ
-
 Corynebacterium glutamicum
2.3.1.35 OATase
-
 Corynebacterium glutamicum
2.3.1.35 ornithine acetyltransferase
-
 Corynebacterium glutamicum
2.6.1.13 OAT
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.13 22
-
 assay at room temperature Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.35 7.5
-
 assay at Corynebacterium glutamicum
2.6.1.13 7.5
-
 assay at Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.13 pyridoxal 5'-phosphate PLP Corynebacterium glutamicum

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.6.1.13 5
-
 pH 7.5, 22°C, recombinant wild-type enzyme Corynebacterium glutamicum L-ornithine

General Information

EC Number General Information Comment Organism
2.3.1.35 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
2.3.1.35 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
2.3.1.35 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
2.6.1.13 metabolism the expression of the genes involved in the arginine operon (argCJBDFGH) for the control of the L-ornithine biosynthesis pathway that is regulated through the binding of ArgR to the so-called ARG operator sites preceding those relevant target genes Corynebacterium glutamicum
2.6.1.13 physiological function the Corynebacterium glutamicum ornithine acetyltransferase (OATase) ArgJ strongly influences the production of L-ornithine by OAT in Corynebacterium glutamicum Corynebacterium glutamicum