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Literature summary extracted from

  • Shu, Q.; Xu, M.; Li, J.; Yang, T.; Zhang, X.; Xu, Z.; Rao, Z.
    Improved L-ornithine production in Corynebacterium crenatum by introducing an artificial linear transacetylation pathway (2018), J. Ind. Microbiol. Biotechnol., 45, 393-404 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.35 gene argJ, recombinant expression of His-tagged enzyme mutant in Escherichia coli strain BL21(DE3), coexpression of exogenous argA from Escherichia coli and argE from Serratia marcescens in Corynebacterium crenatum. The genes EcargAHY and SmargE are inserted in tandem into the pDXW10 plasmid Corynebacterium crenatum

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.35 additional information 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, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method Corynebacterium crenatum

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 crenatum
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate Corynebacterium crenatum SYPA5-5
-
 L-ornithine + N-acetyl-L-glutamate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.35 Corynebacterium crenatum P62058
-
-
2.3.1.35 Corynebacterium crenatum SYPA5-5 P62058
-
-
2.3.1.35 no activity in Escherichia coli
-
-
-

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 crenatum

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.35 recombinant His-tagged enzyme mutant from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Corynebacterium crenatum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.35 additional information OATase activity is measured using a ninhydrin procedure Corynebacterium crenatum ?
-
-
2.3.1.35 additional information OATase activity is measured using a ninhydrin procedure Corynebacterium crenatum SYPA5-5 ?
-
-
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium crenatum L-ornithine + N-acetyl-L-glutamate
-
 ?
2.3.1.35 N2-acetyl-L-ornithine + L-glutamate
-
 Corynebacterium crenatum SYPA5-5 L-ornithine + N-acetyl-L-glutamate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.35 argJ
-
 Corynebacterium crenatum
2.3.1.35 CcOATase
-
 Corynebacterium crenatum
2.3.1.35 L-ornithine acetyltransferase
-
 Corynebacterium crenatum
2.3.1.35 OATase
-
 Corynebacterium crenatum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.35 37
-
 assay at Corynebacterium crenatum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.35 7.4
-
 assay at Corynebacterium crenatum

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 crenatum
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 Corynebacterium crenatum
2.3.1.35 additional information 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 Corynebacterium crenatum