EC Number   |
General Information |
Reference |
|---|
    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) |
-, 756237, 756592, 757355 |
| 2.3.1.35 | malfunction |
enzyme inhibitor pranlukast (PRK) treatment remarkably abates the survival of free as well as macrophage-internalized Mtb, and shows enhanced efficacy in combination with standard-of-care drugs. Notably, PRK also reduces the 5-lipoxygenase (5-LO) signaling in the infected macrophages, thereby surmounting an enhanced response against intracellular pathogen. Further, treatment with PRK alone or with rifampicin leads to significant decrease in Mycobacterium tuberculosis burden and tubercular granulomas in Mtb-infected mice lungs. PRK-mediated killing of Mycobacterium tuberculosis is rescued upon arginine supplementation |
-, 756592 |
| 2.3.1.35 | malfunction |
inactivation of argJ does not cause arginine auxotrophy or marked growth defects |
754657 |
| 2.3.1.35 | metabolism |
ArgJ plays a vital role in the L-citrulline biosynthesis. The enzyme exerts feedback inhibition on N-acetylglutamate synthase, pathway overview |
-, 736594 |
| 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 |
-, 756237 |
| 2.3.1.35 | metabolism |
overexpression of a OTase in Corynebacterium crenatum leads to an improvement of L-Arginine production |
718612 |
| 2.3.1.35 | metabolism |
the enzyme is involved in the arginine biosynthetic pathway |
-, 756592 |
| 2.3.1.35 | metabolism |
the L-ornithine biosynthetic pathway is cyclic due to L-ornithine acetyltransferase (OATase), which catalyzes the conversion of N-acetyl-L-ornithine and L-glutamate to L-ornithine and N-acetyl-Lglutamate (NAG). NAG kinase (NAGK, encoded by argB, EC 2.7.2.8) then phosphorylates NAG in the second step of the pathway. In addition to OATase and NAGK, argC-encoded N-acetyl-L-glutamate 5-semialdehyde dehydrogenase, and argD-encoded N-acetyl-L-ornithine aminotransferase are critical for the conversion of L-glutamate to L-ornithine. These four genes are generally involved in one of the L-arginine synthesis clusters, named argCJBD in Corynebacterium strains |
-, 757355 |
| 2.3.1.35 | more |
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-l-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, lacking a functional ArgJ, to mimic the linear pathway of L-ornithine biosynthesis |
-, 757355 |
| 2.3.1.35 | physiological function |
ArgJ in Mycobacterium tuberculosis is a monofunctional enzyme as it facilitates the transfer of acetyl group to glutamate exclusively from N-acetyl ornithine |
-, 756592 |
