We have studied several properties of rat liver L-threonine deaminase: (1) the affinity for the two substrates, L-serine and L-threonine; (2) the threonine/serine activity ratio which changes with increasing pH; (3) the activation, by pyridoxal 5'-phosphate which is linked to the nonprotonated form of the coenzyme and to at least an -SH group of the enzyme, and (4) the reactivation by pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate after dissociation of the coenzyme. The mechanism of the reactivation by pyridoxamine 5'-phosphate is the most interesting problem opened by the present research.

Pagani, R., Leoncini, R., Pizzichini, M., Vannoni, D., Tabucchi, A., & Marinello, E. (1994). Properties of Rat-Liver L-Threonine Deaminase. ENZYME & PROTEIN, 48(2), 90-97.

Properties of Rat-Liver L-Threonine Deaminase

PAGANI, ROBERTO;LEONCINI, ROBERTO;PIZZICHINI, MARIA;VANNONI, DANIELA;TABUCCHI, ANTONELLA;MARINELLO, ENRICO
1994

Abstract

We have studied several properties of rat liver L-threonine deaminase: (1) the affinity for the two substrates, L-serine and L-threonine; (2) the threonine/serine activity ratio which changes with increasing pH; (3) the activation, by pyridoxal 5'-phosphate which is linked to the nonprotonated form of the coenzyme and to at least an -SH group of the enzyme, and (4) the reactivation by pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate after dissociation of the coenzyme. The mechanism of the reactivation by pyridoxamine 5'-phosphate is the most interesting problem opened by the present research.
Pagani, R., Leoncini, R., Pizzichini, M., Vannoni, D., Tabucchi, A., & Marinello, E. (1994). Properties of Rat-Liver L-Threonine Deaminase. ENZYME & PROTEIN, 48(2), 90-97.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/32363
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