Glyceraldehyde-3-phosphate dehydrogenase fromBacillus stearothermophilus
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چکیده
منابع مشابه
The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.
The binding of NAD+ to glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from Bacillus stearothermophilus has been studied by measurement of protein fluorescence quenching. Slight negative co-operativity was observed in the binding of the third and fourth coenzyme molecules to the tetrameric enzyme. The first two coenzyme molecules were tightly bound. In this respect the enzyme resembles t...
متن کاملAmino Acid Sequence Around the Catalytic Site in Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus.
The tryptic peptide containing the active-site cysteine in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus 1503 was isolated after inhibition of the enzyme with (14)C-iodoacetate. The amino acid sequence of the 20-residue peptide was determined by 19 successive cycles of dansyl-Edman degradation. The sequence shows considerable homology with its counterparts from mesop...
متن کاملMechanism of glyceraldehyde-3-phosphate transfer from aldolase to glyceraldehyde-3-phosphate dehydrogenase.
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...
متن کاملAcetyl phosphate formation catalyzed by glyceraldehyde-3-phosphate dehydrogenase.
Glyceraldehyde-3-phosphate dehydrogenase catalyzes the oxidative phosphorylation of n-glyceraldehyde-3-phosphate to 1,3-diphosphoglyceric acid (1, 2). The enzyme also catalyzes the oxidation of n-glyceraldehyde, although the product of this reaction has not been characterized (1,2). In the present study it is shown that acetaldehyde (3), propionaldehyde, and butyraldehyde also act as substrates...
متن کاملCrystal structure of two ternary complexes of phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus with NAD and D-glyceraldehyde 3-phosphate.
The crystal structure of the phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus was solved in complex with its cofactor, NAD, and its physiological substrate, D-glyceraldehyde 3-phosphate (D-G3P). To isolate a stable ternary complex, the nucleophilic residue of the active site, Cys(149), was substituted with alanine or serine. The C149A and C149S G...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1971
ISSN: 0014-5793
DOI: 10.1016/0014-5793(71)80539-2