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Literature summary for 3.5.4.5 extracted from

  • Vincenzetti, S.; de Sanctis, G.; Costanzi, S.; Cristalli, G.; Mariani, P.; Mei, G.; Neuhard, J.; Natalini, P.; Polzonetti, V.; Vita, A.
    Functional properties of subunit interactions in human cytidine deaminase (2003), Protein Eng., 16, 1055-1061.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F137W/W113F 5-fluorozebularine does not protect mutant enzyme from dissociation by SDS as it does protect the wild-type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
5-fluorozebularine
-
Homo sapiens
SDS wild-type tetramer dissociates into enzymatically inactive monomers, without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inativated monomers restores completely the activity. 5-Fluorozebularine disfavours dissociation of the tetramer into subunits in the wild-type enzyme, but not in the mutant enzyme F137W/W113F Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Subunits

Subunits Comment Organism
More wild-type tetramer dissociates into enzymatically inactive monomers, without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inativated mponomers restores completely the activity Homo sapiens

Synonyms

Synonyms Comment Organism
CDA
-
Homo sapiens