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

BRENDA support

Literature summary extracted from

  • Murphy, D.M.; Ivanenkov, V.V.; Kirley, T.L.
    Identification of cysteine residues responsible for oxidative cross-linking and chemical inhibition of human nucleoside-triphosphate diphosphohydrolase 3 (2002), J. Biol. Chem., 277, 6162-6169.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.5 C10S 112% of wild-type ATPase activity, 105% of wild-type ADPase activity, residue responsible for dimer formation Homo sapiens
3.6.1.5 C10S/C501S 148% of wild-type ATPase activity, 133% of wild-type ADPase activity Homo sapiens
3.6.1.5 C10S/C501S/C509S 79% of wild-type ATPase activity, 77% of wild-type ADPase activity Homo sapiens
3.6.1.5 C10S/C509S 103% of wild-type ATPase activity, 99% of wild-type ADPase activity Homo sapiens
3.6.1.5 C501S 130% of wild-type ATPase activity, 130% of wild-type ADPase activity, site of modification by p-chloromercuriphenylsulfonic acid Homo sapiens
3.6.1.5 C501S/C509S 138% of wild-type ATPase activity, 134% of wild-type ADPase activity Homo sapiens
3.6.1.5 C509S 148% of wild-type ATPase activity, 155% of wild-type ADPase activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.5 additional information not inhibitory: N-ethylmaleimide, iodoacetamide, iodoacetic acid Homo sapiens
3.6.1.5 p-chloromercuriphenylsulfonic acid 1 mM, 56% of inhibition Homo sapiens
3.6.1.5 p-hydroxymercuribenzoate 1 mM, 35% of inhibition Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.5 Homo sapiens
-
-
-

Subunits

EC Number Subunits Comment Organism
3.6.1.5 dimer crosslinking experiments Homo sapiens