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Literature summary extracted from

  • Ahmad, S.; Bhatnagar, R.K.; Venkitasubramanian, T.A.
    Ornithine transcarbamylase from Mycobacterium smegmatis ATCC 14468: purification, properties, and reaction mechanism (1986), Biochem. Cell Biol., 64, 1349-1355.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.3 arginine several arginine analogs have no effect Mycolicibacterium smegmatis
2.1.3.3 L-norvaline competitive vs. ornithine Mycolicibacterium smegmatis
2.1.3.3 ornithine at high concentrations Mycolicibacterium smegmatis
2.1.3.3 phosphate
-
Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.3.3 116000
-
-
Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.3 Mycolicibacterium smegmatis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.3
-
Mycolicibacterium smegmatis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.3 carbamoyl phosphate + L-ornithine = phosphate + L-citrulline mechanism Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.3 carbamoyl phosphate + L-ornithine
-
Mycolicibacterium smegmatis phosphate + L-citrulline
-
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