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Literature summary for 3.6.1.5 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

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

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Subunits

Subunits Comment Organism
dimer crosslinking experiments Homo sapiens