The mechanism of inactivation of S-adenosylhomocysteine hydrolase by fluorinated analogs of 5'-methylthioadenosine.
J Enzyme Inhib
; 13(6): 443-56, 1998 Sep.
Article
em En
| MEDLINE
| ID: mdl-9825307
ABSTRACT
5'-Deoxy-5'-difluoromethylthioadenosine (DFMTA) 1a and 5'-deoxy-5'-trifluoromethyl-thioadenosine (TFMTA) 1b are inhibitors of beef liver S-adenosyl-L-homocysteine hydrolase. DFMTA and TFMTA are time-dependent and irreversible inhibitors of the enzyme. Both 1a and 1b are oxidized by E-NAD+ to produce E-NADH and fluoride anion is formed in the inactivation reaction (2.2 mol of fluoride/mole of enzyme subunit and 3.1 fluoride/mole of enzyme subunit from DFMTA and TFMTA respectively). Using [8-3H]-1a or [8-3H]-1b no trace of labelled adenosine was detected during the inactivation reaction but adenine was formed. The mechanism of inhibition of S-adenosyl-L-homocysteine hydrolase by these two fluorinated nucleosides is discussed.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Tionucleosídeos
/
Adenosina
/
Desoxiadenosinas
/
Inibidores Enzimáticos
/
Hidrolases
Limite:
Animals
Idioma:
En
Revista:
J Enzyme Inhib
Ano de publicação:
1998
Tipo de documento:
Article