Adenosine kinase is an enzyme catalyzing the reaction: adenosine + ATP --> AMP + ADP. We studied some biochemical properties not hitherto investigated and demonstrated that the reaction can be easily reversed when coupled with adenosine deaminase, which transforms adenosine into inosine and ammonia. The overall reaction is: AMP + ADP --> ATP + inosine + NH(3). The exoergonic ADA reaction shifts the equilibrium and fills the energy gap necessary for synthesis of ATP. This reaction could be used by cells under particular conditions of energy deficiency and, together with myokinase activity, may help to restore physiological ATP levels.

Vannoni, D., Giglioni, S., Aceto, E., Marinello, E., Antoro, A., Leoncini, R. (2008). A kinetic study of the rat liver Adenosine Kinase reverse reaction. NUCLEOSIDES, NUCLEOTIDES & NUCLEIC ACIDS, 27(6-7), 872-875 [10.1080/15257770802146544].

A kinetic study of the rat liver Adenosine Kinase reverse reaction

VANNONI, DANIELA;GIGLIONI, STEFANIA;ACETO, EMILIA;MARINELLO, ENRICO;LEONCINI, ROBERTO
2008-01-01

Abstract

Adenosine kinase is an enzyme catalyzing the reaction: adenosine + ATP --> AMP + ADP. We studied some biochemical properties not hitherto investigated and demonstrated that the reaction can be easily reversed when coupled with adenosine deaminase, which transforms adenosine into inosine and ammonia. The overall reaction is: AMP + ADP --> ATP + inosine + NH(3). The exoergonic ADA reaction shifts the equilibrium and fills the energy gap necessary for synthesis of ATP. This reaction could be used by cells under particular conditions of energy deficiency and, together with myokinase activity, may help to restore physiological ATP levels.
Vannoni, D., Giglioni, S., Aceto, E., Marinello, E., Antoro, A., Leoncini, R. (2008). A kinetic study of the rat liver Adenosine Kinase reverse reaction. NUCLEOSIDES, NUCLEOTIDES & NUCLEIC ACIDS, 27(6-7), 872-875 [10.1080/15257770802146544].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/11053
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo