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Literature summary for 3.5.3.1 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

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

Inhibitors

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
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