COENZYME BINDING AND THE THIOL GROUPS OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
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چکیده
منابع مشابه
Coenzyme binding and the thiol groups of glyceraldehyde-3-phosphate dehydrogenase.
Glyceraldehyde-3-phosphate dehydrogenase is inhibited by iodoacetate and under certain conditions it is activated by cysteine and reduced glutathione (1,2). It has therefore been concluded that the enzyme contains thiol groups which are essential for its activity. A relationship between the thiol groups of the enzyme and diphosphopyridine nucleotide (DPN) was first suggested by Rapkine, Rapkine...
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is one of the key redox-sensitive proteins whose activity is largely affected by oxidative modifications at its highly reactive cysteine residue in the enzyme's active site (Cys149). Prolonged exposure to oxidative stress may cause, inter alia, the formation of intermolecular disulfide bonds leading to accumulation of GAPDH aggregates and ultimat...
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Crystals of apo- and holo-D-glyceraldehyde-3-phosphate dehydrogenase from the tail muscle of the Mediterranean lobster Palinurus vulgaris, previously found to be suitable for single crystal microspectrophotometric studies of catalytic activity in the crystalline state, have been examined by x-ray crystallography. The two forms are isomorphous, space group C 2 with cell dimensions a=128.4 A, b=9...
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The high binding affinity of diphosphopyridine nucleotide for glyceraldehyde S-phosphate dehydrogenase was first estimated quantitatively by Velick, Hayes, and Harting (1) by using an ultracentrifugation separation method. A dissociation constant of the order of 10-7 M (2) with a stoichiometry of 3 to 4 moles of DPN+ per mole of enzyme was determined (3). Several characteristics of the apoenzym...
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The catalytic interaction of glyceraldehyde-3-phosphate dehydrogenase with glyceraldehyde 3-phosphate has been examined by transient-state kinetic methods. The results confirm previous reports that the apparent Km for oxidative phosphorylation of glyceraldehyde 3-phosphate decreases at least 50-fold when the substrate is generated in a coupled reaction system through the action of aldolase on f...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1953
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)52326-2