Contrasting behavior of conformationally locked carbocyclic nucleosides of adenosine and cytidine as substrates for deaminases.
Nucleosides Nucleotides Nucleic Acids
; 28(5): 614-32, 2009 May.
Article
en En
| MEDLINE
| ID: mdl-20183605
ABSTRACT
In addition to the already known differences between adenosine deaminase (ADA) and cytidine deaminase (CDA) in terms of their tertiary structure, the sphere of Zn(+2) coordination, and their reverse stereochemical preference, we present evidence that the enzymes also differ significantly in terms of the North/South conformational preferences for their substrates and the extent to which the lack of the O(4') oxygen affects the kinetics of the enzymatic deamination of carbocyclic substrates. The carbocyclic nucleoside substrates used in this study have either a flexible cyclopentane ring or a rigid bicyclo[3.1.0]hexane scaffold.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Adenosina
/
Adenosina Desaminasa
/
Citidina
/
Citidina Desaminasa
Límite:
Animals
Idioma:
En
Revista:
Nucleosides Nucleotides Nucleic Acids
Asunto de la revista:
BIOQUIMICA
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos