Guanosine triphosphate: 5-hydroxylysine phosphotransferase in rat kidney cortex.
An enzyme which catalyzes the transfer of the gamma-phosphate from GTP onto 5-hydroxylysine was partially purified from rat kidney cortex by means of acid precipitation and DEAE-Sephadex A-50 column chromatography. The enzyme activity was assayed by measuring the transfer of [32P] from gamma-[32P]-GTP to materials not adsorbed by charcoal. This partially purified enzyme showed essentially no GTP phosphohydrolase activity and an optimal pH of 8.0. An apparent Km of about 23.8 mumol/1 was obtained with respect to 5-hydroxylysine. Mg2+ was required for the activity of this enzyme. Ethanolamine, L-lysine, L-ornithine and choline inhibited the enzyme but L-threonine, L-serine and hydroxy-L-proline did not. None of these compounds severed as substrate for this enzyme.
D000818:Animals; D006160:Guanosine Triphosphate; D006863:Hydrogen-Ion Concentration; D006901:Hydroxylysine; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D013329:Structure-Activity Relationship
D006901:Hydroxylysine; D006160:Guanosine Triphosphate; D010770:Phosphotransferases; D008274:Magnesium