Vitamin K and phosphate mediated enhancement of brain sulfotransferase activity.
Previous work has shown that vitamin K regulates brain sulfotransferase activity. We now show that activity is lost after treatment with acid phosphatase and is restored with ATP. Orthophosphate activates sulfotransferase to a small degree (26%) with a maximum at 3 mM. Vitamin K1 (or menadione) + orthophosphate stimulates activity 400%; vitamin K alone is not active. ATP activates maximally at 10 mM; ATP + vitamin K increases activation 20%. Protein kinase inhibitors do not affect ATP or orthophosphate + vitamin K mediated activation. Sulfotransferase is inhibited by pyridoxal phosphate indicating modification of a lysyl residue.
Sundaram
K S
KS
Department of Microbiology, CUNY Medical School, New York 10031.
Lev
M
M
D000135:Acid Phosphatase / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001921:Brain / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D051379:Mice; D010710:Phosphates / Q000494:pharmacology*; D010766:Phosphorylation; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D015238:Sulfotransferases / Q000378:metabolism*; D014812:Vitamin K / Q000494:pharmacology*
D010710:Phosphates; D014812:Vitamin K; D011732:Pyridoxal Phosphate; D000255:Adenosine Triphosphate; D015238:Sulfotransferases; D000135:Acid Phosphatase