Dehydrogenases glyceraldehyde 3-phosphate dehydrogenase

Fig. 35. Diagrammatic representation of functionally equivalent groups around the substrate in lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and horse liver alcohol dehydrogenase. From the work of Rossmann and colleagues [164],...

NADH-linked dehydrogenases Glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and alcohol dehydrogenase. 

Analyses of enzyme reaction rates continued to support the formulations of Henri and Michaelis-Menten and the idea of an enzyme-substrate complex, although the kinetics would still be consistent with adsorption catalysis. Direct evidence for the participation of the enzyme in the catalyzed reaction came from a number of approaches. From the 1930s analysis of the mode of inhibition of thiol enzymes—especially glyceraldehyde-phosphate dehydrogenase—by iodoacetate and heavy metals established that cysteinyl groups within the enzyme were essential for its catalytic function. The mechanism by which the SH group participated in the reaction was finally shown when sufficient quantities of purified G-3-PDH became available (Chapter 4). 

Fig. 15. Stereo drawing of a bent helix (glyceraldehyde-phosphate dehydrogenase residues 146-161) with an internal proline. The proline ring produces steric hindrance to the straight a-helical conformation as well as having no NH group available for a hydrogen bond. A proline is the commonest way of producing a bend within a single helix, as well as occurring very frequently at the comers between helices.

Doubly wound variations Glyceraldehyde-phosphate dehydrogenase domain 1 Phosphorylase domain 1, central three layers Flavodoxin... 

Glyceraldehyde-phosphate dehydrogenase domain 2 Bacteriochlorophyll protein p-Hydroxybenzoate hydroxylase domain 2 Influenza virus hemagglutinin HA2 L7/L12 ribosomal protein... 

Domain 1 Greek key helix bundle Domain 2 miscellaneous antiparallel a Dehydrogenases, see Alcohol, Glyceraldehyde phosphate, Malate, or Lactate... 

Domains 1 and 2 doubly wound parallel /3 sheet (Fig. 77) Domain 3 open-face /8 sandwich (Fig. 83) Glyceraldehyde-phosphate dehydrogenase (Buehner et al., 1974) Domain 1 doubly wound parallel /3 sheet (Fig. 77)... 

Fig. 102. Glyceraldehyde-phosphate dehydrogenase domain 2 as an example of an open-face sandwich antiparallel /3 sheet, (a) a-Carbon stereo, viewed from the buried side of the sheet (b) backbone schematic, viewed as in a.

Tyrosyl-tRNA synthetase dl, d2 Thermolysin dl, d2 T4 phage lysozyme dl, d2 Glucosephosphate isomerase dl, d2 Pyruvate kinase dl, d2 Pyruvate kinase d2, d3 Lactate dehydrogenase dl, d2 Alcohol dehydrogenase dl, d2 Glyceraldehyde-phosphate dehydrogenase dl,d2... 

Glyceraldehyde-phosphate dehydrogenase arsenate and, 44 193-194 Glycerol, as matrix liquid, 28 5 Glyceiol-3-phosphate dehydrogenase, 44 206, 207... 

Brune and Lapetina (1989) reported that NO could activate a platelet ADP-ribosyltransferase that resulted in the ribosylation of a 39 kDa protein. Subsequent work revealed that the protein was glyceraldehyde phosphate dehydrogenase (GAP-DH), and that ribosylation was associated with reduced GAP-DH activity (Dimmeler et al., 1992). In our collaboration with Molina et al., (1992), we have shown that GAP-DH activity is dramatically inhibited in C. parvum treated rats and that this action is associated with both a ribosylation and nitro-sylation of the enzyme. Such a marked inhibition of a glycolytic enzyme could explain some of the metabolic changes observed in the liver in sepsis. 

The idea that enzymes whose normal substrate is orthophosphate can use arsenate in its place, and that the esters of arsenate formed are rapidly hydrolyzed, was given by Braunstein (16) in 1931, to explain the effects of arsenate on glycolysis. This idea was formulated more precisely for glyceraldehyde-phosphate dehydrogenase in 1939. This enzyme, E—SH, normally oxidizes its aldehyde substrate with phosphate uptake to give an acyl phosphate, as follows ... 

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+.

Figure 3-10 Estimation of the molecular mass of the polypeptide chain of the nitrogenase Fe-protein using SDS-poly-acrylamide electrophoresis from a set of four standard curves. The marker proteins are (1) catalase, (2) fumarase, (3) aldolase, (4) glyceraldehyde-phosphate dehydrogenase, (5) a-chymotrypsinogen A, and (6) myoglobin, (o) indicates position of azoferredoxin. From Nakos and Mortenson.195...

Another assay for phosphoffuctokinase involves converting the fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate with aldolase, equilibrating the triosephosphates with triosephosphate isomerase, and then measuring the production of NADH on the oxidation of the glyceraldehyde phosphate by glyceraldehyde 3-phosphate dehydrogenase. 

Aside from PEPCase, a number of other CAM-related genes have been partially characterised (Table 1). These include cDNA clones for pyruvate, orthophosphate dikinase (PPDK), a specific NADP malate dehydrogenase (MDH), glyceraldehyde phosphate dehydrogenase (GaPDH) and NADP-dependent malic enzyme (MOD). Previous studies indicated that the enzymatic activities of these gene products increased upon salt stress in the ice plant (Holtum Winter, 1982). As in the case... 

A V- - NAD+ Triosephosphate Isomerase y"— NADH Glyceraldehyde Phosphate Dehydrogenase 1,3-Bisphosphoglycerate A U -ADP... 

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. 

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