A-Phosphoglycerate

F5. Fujii, H., Krietsch, W. K. G., and Yoshida, A., A single amino acid substitution (Asp -> Asn) in a phosphoglycerate kinase variant (PGK Miinchen) associated with enzyme deficiency. J. Biol. Chem. 255,6421-6423 (1980). 

F8. Fujii, H., Chen, S.-H., Akatsuka, J Miwa, S., and Yoshida, A., Use of cultured lymphoblastoid cells for the study of abnormal enzymes Molecular abnormality of a phosphoglycerate kinase variant associated with hemolytic anemia. Proc. Natl. Acad. Sci. U.S.A. 78,2587-2590 (1981). 

M2. Maeda, M and Yoshida, A., Molecular defect of a phosphoglycerate kinase variant (PGK-Mat-sue) associated with hemolytic anemia Leu - Pro substitution caused by T/A - C/G transition in exon 3. Blood 77, 1348-1352(1991). 

M3. Maeda, M., Bawle, E. V., Kulkami, R Beutler, E., and Yoshida, A., Molecular abnormality of a phosphoglycerate kinase variant generated by spontaneous mutation. Blood 79,2759-2762 (1992). 

Ookawara, T., Dave, V., Willems, P Martin, J.-J., de Barsy, T., Matthys, E., and Yoshida, A., Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant. Arch. Biochem. Biophys. 327, 35-40 (1996). 

T26. Turner, G., Fletcher, J., Elber, J., Yanagawa, Y Dav6, V., and Yoshida, A., Molecular defect of a phosphoglycerate kinase variant associated with haemolytic anaemia and neurological disorders in a large kindred. Br. J. Haematol. 91,60-65 (1995). 

SCHEME 8.4 Solid-phase synthesis methodology to attach a phosphoglycerate lipid unit to an elaborated disaccharide and cleavage from solid support. 

Dehydration reactions occur in many important biological processes. Instead of being catalyzed by strong acids, which would not be available to a cell, they are catalyzed by enzymes. Enolase, for example, catalyzes the dehydration of a-phosphoglycerate in glycolysis. Glycolysis is a series of reactions that prepare glucose for entry into the citric acid cycle (Section 25.7). 

The net result of photosynthesis is reduction of carbon dioxide to form carbohydrates. A key intermediate is phosphoglyceric acid, from which various simple sugars are produced and disproportionated to form other carbohydrates. 

Figure 6 Apparent elastic incoherent structure factor A q(Q) for ( ) denatured and ( ) native phosphoglycerate kinase. The solid line represents the fit of a theoretical model in which a fraction of the hydrogens of the protein execute only vihrational motion (this fraction is given by the dotted line) and the rest undergo diffusion in a sphere. For more details see Ref. 25.

The stmcture was determined to 2.8 A resolution in the laboratory of Tom Steitz, Yale University, (d) The glycolytic enzyme phospho-glycerate mutase, which catalyzes transfer of a phos-phoryl group from carbon 3 to carbon 2 In phosphoglycerate. The structure was determined to 2.S A resolution in the laboratory of Herman Watson, Bristol University, UK. (Adapted from J. Richardson.)... 

FIGURE 6.28 Examples of protein domains with different numbers of layers of backbone strnctnre. (a) Cytochrome c with two layers of a-helix. (b) Domain 2 of phosphoglycerate kinase, composed of a /3-sheet layer between two layers of helix, three layers overall, (c) An nnnsnal five-layer strnctnre, domain 2 of glycogen phosphorylase, a /S-sheet layer sandwiched between four layers of a-helix. (d) The concentric layers of /S-sheet (inside) and a-helix (outside) in triose phosphate isomerase. Hydrophobic residnes are bnried between these concentric layers in the same manner as in the planar layers of the other proteins. The hydrophobic layers are shaded yellow. (Jane Richarelson)... 

FIGURE 19.24 A mechanism for the phosphoglycerate mutase reaction in rabbit muscle and in yeast. Zelda Rose of the Institute for Cancer Research in Philadelphia showed that the enzyme requires a small amount of 2,3-BPG to phosphorylate the histidine residue before the mechanism can proceed. Prior to her work, the role of the phosphohistidine in this mechanism was not understood. 

A different mechanism operates in the wheat germ enzyme. 2,3-Bisphosphoglycerate is not a cofactor. Instead, the enzyme carries out intra-molecular phosphoryl group transfer (Figure 19.25). The C-3 phosphate is transferred to an active-site residue and then to the C-2 position of the original substrate molecule to form the product, 2-phosphoglycerate. 

Each number in parentheses represents the number of carbon atoms in a compound, and the number preceding the parentheses indicates the stoichiometry of the reaction. Thus, 6(1), or 6 COg, condense with 6(5) or 6 RuBP to give 12 3-phosphoglycerates. These 12(3)s are then rearranged in the Calvin cycle to form one hexose, 1 (6), and regenerate the six 5-carbon (RuBP) acceptors. 

C-labeled carbon dioxide is administered to a green plant, and shortly thereafter the following compounds are isolated from the plant 3-phosphoglycerate, glucose, erythrose-4-phosphate, sedoheptulose-l,7-bisphosphate, ribose-5-phosphate. In which carbon atoms will radioactivity be found ... 

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