[Comparative study of glutamate dehydrogenases of Chlorella].
The kinetic properties of the constitutive double specific glutamate dehydrogenase (NAD(P)--GDH) and the inducible NADP-specific glutamate dehydrogenase (NADP--GDH) of Chlorella pyrenoidosa Pringsheim 82T (thermophilic strain) in a deaminating reaction have been studied. NAD(P)-GDH behaves in a deamination as a Michaelis-Menten enzyme. NADP-GDH displays some lag-period before a steady-state phase. The duration of this lag depends on a substrate concentration. Besides that, an effect of all the substrates on a heat inactivation of both GDH and a product inhibition have been studied. All the substrates except the reduced co-factors protect effectively GDH from the heat inactivation, especially the thermolabille NADP-GDH. On the contrary, NAD(P)-H promote the heat inactivation of both GDH. The product inhibition analysis shows that the inducible NADP-GDH acts in vivo as a synthetic enzyme. In the previous paper (V. R. Shatilov et all., 1974, Dokl. Acad. Nauk USSR, 216,223) it was shown for the constitutive GDH that p-CMB strongly inhibited a desamination and slightly (if any) affect an amination. It this paper it is shown that action of p-CMB on the amination depends on the presence of NAD+ (not NADP+ or L-glutamate). p-CMB and NAD+ affect tha amination in a strongly sunergetic manner. Some suggestions about the intracellular localization of chlorella GDH are made.
D002708:Chlorella / Q000201:enzymology*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D009243:NAD / Q000494:pharmacology; D009249:NADP / Q000494:pharmacology
D002729:Chloromercuribenzoates; D007527:Isoenzymes; D009243:NAD; D009249:NADP; D005969:Glutamate Dehydrogenase
Sravnitel'noe izuchenie glutamatdegidrogenaz khlorelly