Purification and steady state kinetic mechanism of glycogen synthase-D from human polymorpho-nuclear leukocytes.
The authors' work on the purification and steady state kinetic investigation of the enzyme glycogen synthase D (UDP-glucose: glycogen 4-alpha-glucosyl-transferase, EC 2.4.1.11) from human polymorphonuclear leukocytes is reviewed. The main features of the kinetic mechanism for catalysis of the reaction interconversion of the quaternary enzyme-substrate-activator complexes. The anions interact exclusively with the G-6-P binding site of the enzyme. The dissociation constants for the enzyme-modifier complexes are determined, and a kinetic mechanism for the action of the anions is proposed, leading to activation or inhibition, depending on the concentration of G-6-P.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D006006:Glycogen Synthase / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008433:Mathematics; D009504:Neutrophils / Q000201:enzymology*; D009994:Osmolar Concentration; D012965:Sodium Chloride / Q000494:pharmacology
D007527:Isoenzymes; D008345:Manganese; D012965:Sodium Chloride; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D006006:Glycogen Synthase; D008274:Magnesium; D002118:Calcium