Glyceraldehyde-phosphate structure

Figure 2-13 (A) Stereoscopic view of the nucleotide binding domain of glyceraldehyde phosphate dehydrogenase. The enzyme is from Bacillus stearothermophilus but is homologous to the enzyme from animal sources. Residues are numbered 0-148. In this wire model all of the main chain C, O, and N atoms are shown but side chains have been omitted. The large central twisted P sheet, with strands roughly perpendicular to the page, is seen clearly hydrogen bonds are indicated by dashed lines. Helices are visible on both sides of the sheet. The coenzyme NAD+ is bound at the end of the P sheet toward the viewer. Note that the two phosphate groups in the center of the NAD+ are H-bonded to the N terminus of the helix beginning with RIO. From Skarzynski et al.llla (B) Structural formula for NAD+.

A similar conclusion was arrived at by Arnold and Pette ( 2) from studies carried out on the in vitro binding of aldolase glyceraldehyde phosphate dehyrogenase, fructose-6-phosphate kinase, phosphoglycerate kinase, pyruvate kinase and lactate dehydrogenase to the structural proteins F-actin, myosin, acto-myosin and stromaprotein. 

Deoxy-D-xylulose is a known natural product. It was first isolated from the fermentation broth of a Streptomyces and later shown to be a precursor of pyridoxol. Its structure can be deduced biogenetically from pyruvate and glyceraldehyde phosphate (Figs. 2 and 3). Two H-labeled DX isotopomers were synthesized chemically. They were incorporated efficiently into the prenyl chains of ubiquinone and menaquinone by wild-type E. coli, indicating that a DX derivative is an isoprenoid precursor (2, 3). 

Triosephosphate isomerase is involved in the glycolytic pathway, and catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde phosphate (Fig. 17-27). The refined three-dimensional structures of chicken, yeast, and trypano-... 

Zinc is essential for the functioning of at least twenty different enzymes, and their functions are widely varied. They include the alcohol dehydrogenases of yeast and mammalian liver, glyceraldehyde phosphate dehydrogenase, phosphoglycomutase of yeast, DNA and RNA polymerases (at least in bacteria), alkaline phosphatase in bacteria, mammalian carbo-xypeptidase, carbonic anhydrase, AMP hydrolase, pyruvate carboxylase (yeast), and aldolase (yeast and bacteria). The alkaline phosphatase of E, coli has, in each molecule, four atoms of zinc the two which maintain structure can be replaced by Mn, Co +, or Cu, whereas the other two atoms are essential for enzyme action (Trotman and Greenwood, 1971). 

Suggest a reasonable structure for the intermediate in the con ] version of dihydroxyacetone phosphate to o glyceraldehyde 3 phosphate J... 

FIGURE 6.34 Sheet structures formed from andparallel arrangements of /3-strands, (a) Streptomyces suh i x Xu inhibitor, (b) glutathione reductase domain 3, and (c) the second domain of glyceraldehyde-3-phosphate dehydrogenase represent minimal andparallel /S-sheet domain structures. In each of these cases, an andparallel /S-sheet is largely exposed to solvent on one face and covered by helices and random coils on the other face. (Jane Richardson)... 

R)-Glyceraldehyde. Fischer projection of, 976 molecular model of, 976, 977 Glyceric acid, structure of. 753 Glycerol, catabolism of, 1132-1133 s/i-Glycerol 3-phosphate, naming of, 1132... 

Outline in detail, using structural formulas, the enzyme-catalyzed reactions by which cells in the human body convert glyceraldehyde 3-phosphate into pyruvate. 

The aldehyde ferredoxin oxidoreductase from the hyperthermophile Pyrococcus furiosus was the first molybdopterin-dependent enzyme for which a three-dimensional structure became available.683,684 The tungstoenzyme resembles that of the related molybdo-enzyme (Fig. 16-31). A similar ferredoxin-dependent enzyme reduces glyceraldehyde-3-phosphate.685 Another member of the tungstoenzyme aldehyde oxidoreductase family is carboxylic acid reductase, an enzyme found in certain acetogenic clostridia. It is able to use reduced ferredoxin to convert unactivated carboxylic acids into aldehydes, even though E° for the acetaldehyde/acetate couple is -0.58 V.686... 

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