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Properties of rat liver L-threonine deaminase
R Pagani1, R Leoncini, M Pizzichini
1Institute of Biochemistry and Enzymology, University of Siena, Italy.
Enzyme & Protein
|January 1, 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.