Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Colleluori, D.M.; Reczkowski, R.S.; Emig, F.A.; Cama, E.; Cox, J.D.; Scolnick, L.R.; Compher, K.; Jude, K.; Han, S.; Viola, R.E.; Christianson, D.W.; Ash, D.E.
    Probing the role of the hyper-reactive histidine residue of arginase (2005), Arch. Biochem. Biophys., 444, 15-26.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.1 additional information mutation of H141 to study its role in catalysis Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.1 diethyl dicarbonate second-order rate constant of 113 per M and s for inactivation process. L-ornithine partially protects, L-ornithine plus borate completely protect Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.1 Rattus norvegicus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.3.1 L-arginine + H2O = L-ornithine + urea H141 serves as an acid/base catalyst, deprotonating the metal-bridging water molecule to generate the metal-bridging hydroxide nucleophile, and by protonating the amino group of the product to facilitate its departure Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.3.1 liver
-
Rattus norvegicus
-