Adenosine deaminase from Saccharomyces cerevisiae: kinetics and interaction with transition and ground state inhibitors.
Biochim Biophys Acta
; 1122(3): 311-6, 1992 Aug 21.
Article
en En
| MEDLINE
| ID: mdl-1504093
ABSTRACT
Several adenosine analogs, such as coformycin, 2'-deoxycoformycin and erythro-9-(3-nonyl-p-aminobenzyl)adenine (EHNA), which are strong inhibitors of mammalian adenosine deaminase, are much weaker inhibitors of the Saccharomyces cerevisiae enzyme. The specificity of the yeast enzyme is more restricted than that of mammalian adenosine deaminase, particularly towards the ribose moiety and around position 6 and 1 of the substrate. The sulphydryl group appears to be more masked in the yeast than in the mammalian enzyme. The kinetic effects of pH with adenosine substrate and with the inhibitor purine riboside are reported. The findings on specificity and pH kinetic effects can be interpreted in a model involving proton transfer from the -SH group of the enzyme to the N-1 atom of the substrate.
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Banco de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Adenosina Desaminasa
Tipo de estudio:
Prognostic_studies
Idioma:
En
Año:
1992
Tipo del documento:
Article