Kinetic study on the dimer-tetramer interconversion of glycogen phosphorylase a.
Eur J Biochem
; 259(3): 609-17, 1999 Feb.
Article
em En
| MEDLINE
| ID: mdl-10092844
ABSTRACT
Kinetic theory of dissociating enzyme systems has been applied to a study of the dimer-tetramer interconversion of glycogen phosphorylase a. All kinetic constants for the dissociating-associating reaction of phosphorylase a have been determined. The results indicate that (a) the presence of glucose-1-phosphate has no influence on either the rate of dissociation or the rate of association, and hence does not shift the dimer-tetramer equilibrium of phosphorylase a; (b) the binding og glycogen to the enzyme decreases the association rate of the dimer to form the tetramer, but has no effect on the dissociation rate of the tetramer; (c) both the dimeric and tetrameric form of phosphorylase a can bind glycogen, but the tetrameric form has a lower affinity for glycogen and is catalytically inactive.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosforilase a
/
Conformação Proteica
Idioma:
En
Revista:
Eur J Biochem
Ano de publicação:
1999
Tipo de documento:
Article