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 [10.1159/000474974].
Properties of Rat-Liver L-Threonine Deaminase
Pagani R.;Leoncini R.;Pizzichini M.;Vannoni D.;Tabucchi A.;Marinello E.
1994-01-01
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.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/32363
Attenzione
Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo