Sphingolipid base metabolism. Partial purification and properties of sphinganine kinase of brain.
The presence of sphinganine kinase in bovine brain has been demonstrated. The product of the action of the brain enzyme on sphinganine has been characterized as sphingamine 1-phosphate by a combination of chemical, enzymatic, and chromatographic techniques. The bovine brain enzyme has been partially purified and appears to exist in multiple forms. The molecular weight of the most highly purified preparation of the enzyme was estimated to be 190,000 by gel filtration. The purified form of the enzyme showed highest activity with ATP but was also active with other purine nucleoside triphosphates. UTP and CTP did not serve as substrates for the enzyme.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D004355:Drug Stability; D007700:Kinetics; D008970:Molecular Weight; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D013107:Sphingolipids / Q000378:metabolism*; D013110:Sphingosine / Q000031:analogs & derivatives; D013329:Structure-Activity Relationship
D013107:Sphingolipids; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022647:sphinganine kinase; D013110:Sphingosine