Kinases phosphoglycerate kinase

Hexokinase Pyruvate kinase Adenylate kinase Phosphoglycerate kinase Phosphofructokinase Protease inhibitors Pancreatic trypsin inhibitor Soybean trypsin inhibitor Streptomyces subtilisin inhibitor Nucleases... 

ADP as a substrate in enzyme reactions, ADENYLATE KINASE (or MYOKINASE) ATP SYNTHASE CREATINE KINASE NUCLEOSIDE DIPHOSPHATE KINASE PHOSPHOGLYCERATE KINASE PYRUVATE KINASE RIBONUCLEOTIDE REDUCTASE SULFATE ADENYLYLTRANSFERASE (ADP) [ADP]/[ATP] ratio,... 

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. 

The iPocp) folding unit occurs in many proteins. It is the essential structure of oc/p proteins, a common structure of dehydrogenases (alcohol dehydrogenase, lactate dehydrogenase), some kinases (hexokinase, adenylate kinase, phosphoglycerate kinase), and phosphoglycerate mutase. It is also found in carbonic anhydrase, carboxypeptidase A, cytochrome 65, flavodoxin, papain, rhodanese, thioredoxin, and subtilisin. 

The Rossmann fold is also a conservative structure. Such a structure, which consists of parallel strands of p sheets flanked by two helices on each side which are antiparallel with regard to the sheets, is found in NAD dehydrogenases, in several kinases (e.g., adenylate kinase, phosphoglycerate kinase), and in all enzymes which have a coenzyme with a nucleotide part, NAD+ or ATP. 

Example Change in Dynamics on Denaturing Phosphoglycerate Kinase... 

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.

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)... 

Glycolysis Glyceraldehyde-3-phosphate dehydrogenase Phosphoglycerate kinase Pyruvate kinase... 

Fig. 3. Three-dimensional model of human phosphoglycerate kinase based on the structure of horse enzyme. Positions of the molecular abnormalities of variant enzymes are also shown.

Hereditary deficiency of phosphoglycerate kinase (PGK) is associated with hereditary hemolytic anemia and often with central nervous system dysfunction and/or myopathy. The first case, reported by Kraus et al. (K24), is a heterozygous female, and the results are not so clear. The second family, reported by Valentine et al. (V3), is a large Chinese family, whose pedigree study indicates that PGK deficiency is compatible with X-linked inheritance. To date, 22 families have been reported (04, T25, Y3). Nine of these have manifested both symptoms five have shown only hemolysis seven have shown the central nervous system dysfunction and/or myopathy but without hemolysis and one case, PGK Munchen, is without clinical symptoms (F5). PGK II is an electrophoretic variant found in New Guinea populations (Y2). Red blood cell enzyme activity, specific activity, and the kinetic properties of this polymorphic variant are normal. 

Cl2. Cohen-Solal, M., Valentin, C., Plassa, F., Guillemin, G Danze, F., Jaisson, F., and Rosa, R., Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes PGK Crdteil and PGK Amiens. Blood 84,898-903 (1994). 

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). 

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