The interaction and inhibition of muscle lactate dehydrogenase by the alkaloid caffeine.
Biochem Biophys Res Commun
; 127(3): 1057-65, 1985 Mar 29.
Article
em En
| MEDLINE
| ID: mdl-3985952
ABSTRACT
Kinetic analysis showed that the alkaloid caffeine is a competitive inhibitor of the enzyme lactate dehydrogenase with respect to substrate pyruvate, and a non-competitive inhibitor with respect to the coenzyme NADH. The inhibitor constant Ki is 0,54 mM. Scatchard analysis determined the dissociation constant for a single independent binding site of the ternary lactate dehydrogenase - NADH - caffeine complex (KE-NADH-CAFFEINE) and the number of binding sites to be 0,14 mM and 3,83 respectively. Caffeine binds to a hydrophobic domain in the substrate binding site. Alternate nucleophilic - electrophilic functionalities within the inhibitor molecule are proposed to be the fundamental reason for the inhibition.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cafeína
/
L-Lactato Desidrogenase
/
Músculos
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1985
Tipo de documento:
Article