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Literature summary extracted from

  • Dou, W.; Xu, M.; Cai, D.; Zhang, X.; Rao, Z.; Xu, Z.
    Improvement of L-arginine production by overexpression of a bifunctional ornithine acetyltransferase in Corynebacterium crenatum (2011), Appl. Biochem. Biotechnol., 165, 845-855.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.35 expressed in Escherichia coli Corynebacterium crenatum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.35 39700
-
 calculated from cDNA Corynebacterium crenatum

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.35 Corynebacterium crenatum C1KGU6 functional study reveals that OATase from Corynebacterium crenatum SYPA5-5 is a bifunctional enzyme with the functions of acetylglutamate synthase and acetylornithine deacetylase
-

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 crenatum L-ornithine + N-acetyl-L-glutamate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.35 heterodimer alpha- and beta-subunits can not self-assemble to active OATase conformation Corynebacterium crenatum

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.35 30
-
 assay at Corynebacterium crenatum

pH Optimum

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

General Information

EC Number General Information Comment Organism
2.3.1.35 metabolism overexpression of a OTase in Corynebacterium crenatum leads to an improvement of L-Arginine production Corynebacterium crenatum