Aliphatic diamines exert a dead-end inhibition on the S-adenosylmethionine dependent indolethylamine-N-methyltransferase from rabbit lung Kinetic studies show that this inhibition is uncompetitive with respect to S-adenosylmethionine and competitive with respect to tryptamine. The Ki values of the most effective diaminic inhibitors (1,8-diaminooctane and 1,7-diaminoheptane) indicate a similar affinity to tryptamine for the enzyme. A reaction mechanism “Ordered BiBi” with S-adenosylmethionine as first substrate bound is suggested.
Inhibition of indolethylamine-N-methyltransferase by aliphatic diamines / Porta, Raffaele; M., Camardella; C., Esposito; G., Della Pietra. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 77:(1977), pp. 1196-1202. [10.1016/S0006-291X(77)80106-X]
Inhibition of indolethylamine-N-methyltransferase by aliphatic diamines.
PORTA, RAFFAELE;
1977
Abstract
Aliphatic diamines exert a dead-end inhibition on the S-adenosylmethionine dependent indolethylamine-N-methyltransferase from rabbit lung Kinetic studies show that this inhibition is uncompetitive with respect to S-adenosylmethionine and competitive with respect to tryptamine. The Ki values of the most effective diaminic inhibitors (1,8-diaminooctane and 1,7-diaminoheptane) indicate a similar affinity to tryptamine for the enzyme. A reaction mechanism “Ordered BiBi” with S-adenosylmethionine as first substrate bound is suggested.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
