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Glyceraldehyde dehydrogenase

Figure 3.1 Amino add side-chain groups involved in binding NAD at the active site of an enzyme. The enzyme is glyceraldehyde dehydrogenase. More than 20 amino acids, the position of which in the primary structure is indicated by the number, counting from the N-terminal amino acid, are involved in the binding. This emphasises the complexity of the binding that is responsible for the specificity of the enzyme for NAD (depicted in bold). The molecular structure of nicotinamide adenine dinucleotide (NAD ) provided in Appendix 3.3. Figure 3.1 Amino add side-chain groups involved in binding NAD at the active site of an enzyme. The enzyme is glyceraldehyde dehydrogenase. More than 20 amino acids, the position of which in the primary structure is indicated by the number, counting from the N-terminal amino acid, are involved in the binding. This emphasises the complexity of the binding that is responsible for the specificity of the enzyme for NAD (depicted in bold). The molecular structure of nicotinamide adenine dinucleotide (NAD ) provided in Appendix 3.3.
It has recently been shown that oxidative damage to glyceraldehyde dehydrogenase (GDH), an important glycolytic enzyme, occurs in the frontal cortex in PD patients (Gomez and Ferrer, 2009). Not only would this limit ATP synthesis and generation of many necessary metabolic... [Pg.116]

DHAP is a glycolysis intermediate, whereas glyceraldehyde must be reduced by a mitochondrial enzyme, glyceraldehyde dehydrogenase, to glycerol, which is then subject to action by glycerol kinase in the liver. The aldolase seems to be the principal pathway of metabolizing fructose and depends on the initial phosphorylation step catalyzed by fructokinase, which produces fructose-l-phosphate. Fructokinase is defective in an inherited disorder, essential fructosuria. Fructose-l-phosphate aldolase is deficient in the hereditary disorder fructose intolerance. [Pg.487]

Thermostable enzymes are not always best suited for desired industrial enzymatic activities and specific activities. A key challenge for synthetic enzymatic pathways, for example, is ensuring that optimal enzyme activity for all enzymes is in the same temperature window to avoid kinetic limitations. Moreover, product inhibition has been observed. To address these issues, thermostable enzymes have been engineered. A prime example includes the characterization of two enzymes, glyceraldehyde dehydrogenase and alcohol dehydrogenase, which... [Pg.810]

Stefiler, F. and Sieber, V. (2013) Refolding of a thermostable glyceraldehyde dehydrogenase for application in synthetic cascade biomanufacturing. PLoS One, 8, e70592. [Pg.820]

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)... [Pg.190]

Thus far, we have considered enzyme-catalyzed reactions involving one or two substrates. How are the kinetics described in those cases in which more than two substrates participate in the reaction An example might be the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (Chapter 19) ... [Pg.454]

FIGURE 16.10 Formation of a covalent intermediate in the glyceraldehyde-3-phos-phate dehydrogenase reaction. Nucleophilic attack by a cysteine —SH group forms a covalent acylcysteine intermediate. Following hydride transfer to NAD, nucleophilic attack by phosphate yields the product, 1,3-bisphosphoglycerate. [Pg.510]

FIGURE 19.18 A mechanism for the glycer-aldehyde-3-phosphate dehydrogenase reaction. Reaction of an enzyme snlfliydryl with the carbonyl carbon of glyceraldehyde-3-P forms a thiohemiacetal, which loses a hydride to NAD to become a thloester. Phosphorolysls of this thloester releases 1,3-blsphosphoglycerate. [Pg.625]

FIGURE 19.30 (a) Pyruvate reduction to ethanol in yeast provides a means for regenerating NAD consumed in the glyceraldehyde-3-P dehydrogenase reaction, (b) In oxygen-depleted muscle, NAD is regenerated in the lactate dehydrogenase reaction. [Pg.631]

How might iodoacetic acid affect the glyceraldehyde-3-phosphate dehydrogenase reaction in glycolysis Justify your answer. [Pg.637]

NAD (P) " -dependent enzymes are stereospecific. Malate dehydrogenase, for example, transfers a hydride to die pro-/ position of NADH, whereas glyceraldehyde-3-phosphate dehydrogenase transfers a hydride to die pro-5 position of the nicotinamide. Alcohol dehydrogenase removes a hydride from the pro-i position of edianol and transfers it to die pro-i position of NADH. [Pg.656]

Most of the NADH used in electron transport is produced in the mitochondrial matrix space, an appropriate site because NADH is oxidized by Complex I on the matrix side of the inner membrane. Furthermore, the inner mitochondrial membrane is impermeable to NADH. Recall, however, that NADH is produced in glycolysis by glyceraldehyde-3-P dehydrogenase in the cytosol. If this NADH were not oxidized to regenerate NAD, the glycolytic pathway would cease to function due to NAD limitation. Eukaryotic cells have a number of shuttle systems that harvest the electrons of cytosolic NADH for delivery to mitochondria without actually transporting NADH across the inner membrane (Figures 21.33 and 21.34). [Pg.702]

Calculate the value of A l,/ for the glyceraldehyde-3-phos-phate dehydrogenase reaction, and calculate the free energy change for the reaction under standard-state conditions. [Pg.706]

As discussed in Section 22.7, illumination of chloroplasts leads to light-driven pumping of protons into the thylakoid lumen, which causes pH changes in both the stroma and the thylakoid lumen (Figure 22.27). The stromal pH rises, typically to pH 8. Because rubisco and rubisco activase are more active at pH 8, COg fixation is activated as stromal pH rises. Fructose-1,6-bisphosphatase, ribulose-5-phosphate kinase, and glyceraldehyde-3-phosphate dehydrogenase all have alkaline pH optima. Thus, their activities increase as a result of the light-induced pH increase in the stroma. [Pg.736]


See other pages where Glyceraldehyde dehydrogenase is mentioned: [Pg.159]    [Pg.811]    [Pg.119]    [Pg.960]    [Pg.185]    [Pg.84]    [Pg.12]    [Pg.106]    [Pg.337]    [Pg.79]    [Pg.111]    [Pg.111]    [Pg.410]    [Pg.159]    [Pg.811]    [Pg.119]    [Pg.960]    [Pg.185]    [Pg.84]    [Pg.12]    [Pg.106]    [Pg.337]    [Pg.79]    [Pg.111]    [Pg.111]    [Pg.410]    [Pg.446]    [Pg.44]    [Pg.108]    [Pg.641]    [Pg.538]    [Pg.170]    [Pg.189]    [Pg.427]    [Pg.614]    [Pg.624]    [Pg.624]    [Pg.624]    [Pg.624]    [Pg.656]    [Pg.733]    [Pg.735]    [Pg.747]    [Pg.1148]    [Pg.1163]    [Pg.673]   
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Acyl-enzyme in glyceraldehyde phosphate dehydrogenase

Amino acid glyceraldehyde-3-phosphate dehydrogenases

Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase

Brain glyceraldehyde-3-phosphate dehydrogenase

Cooperativity, glyceraldehyde-3-phosphate dehydrogenase

Crystal structure glyceraldehyde-3-phosphate dehydrogenase

Cysteine residues glyceraldehyde-3-phosphate dehydrogenase

Dehydrogenases glyceraldehyde-3-phosphate dehydrogenase

Enzymes glyceraldehyde 3-phosphate dehydrogenase

Erythrocytes glyceraldehyde-3-phosphate dehydrogenase

Fermentation glyceraldehyde-3-phosphate dehydrogenase

Fluorescence glyceraldehyde-3-phosphate dehydrogenase

Glyceraldehyd

Glyceraldehyd dehydrogenase

Glyceraldehyd dehydrogenase

Glyceraldehyde 3-phosphate dehydrogenase and

Glyceraldehyde 3-phosphate dehydrogenase formation of NADH

Glyceraldehyde 3-phosphate dehydrogenase in fermentation reactions

Glyceraldehyde 3-phosphate dehydrogenase in oxidation of aldehydes

Glyceraldehyde 3-phosphate dehydrogenase thiol group

Glyceraldehyde phosphate dehydrogenase

Glyceraldehyde phosphate dehydrogenases

Glyceraldehyde-3-phosphate dehydrogenase (EC

Glyceraldehyde-3-phosphate dehydrogenase GAPDH)

Glyceraldehyde-3-phosphate dehydrogenase active site

Glyceraldehyde-3-phosphate dehydrogenase amino acid modification

Glyceraldehyde-3-phosphate dehydrogenase catalysis

Glyceraldehyde-3-phosphate dehydrogenase dissociation and hybridization

Glyceraldehyde-3-phosphate dehydrogenase distribution

Glyceraldehyde-3-phosphate dehydrogenase function

Glyceraldehyde-3-phosphate dehydrogenase human

Glyceraldehyde-3-phosphate dehydrogenase inhibition

Glyceraldehyde-3-phosphate dehydrogenase inhibitors

Glyceraldehyde-3-phosphate dehydrogenase isolation

Glyceraldehyde-3-phosphate dehydrogenase mechanism

Glyceraldehyde-3-phosphate dehydrogenase mechanism of action

Glyceraldehyde-3-phosphate dehydrogenase mesophiles

Glyceraldehyde-3-phosphate dehydrogenase metabolic role

Glyceraldehyde-3-phosphate dehydrogenase modification

Glyceraldehyde-3-phosphate dehydrogenase other activities

Glyceraldehyde-3-phosphate dehydrogenase reaction catalyzed

Glyceraldehyde-3-phosphate dehydrogenase sequence

Glyceraldehyde-3-phosphate dehydrogenase structure

Glyceraldehyde-3-phosphate dehydrogenase tissues

Glyceraldehyde-3-phosphate dehydrogenase, G3PDH

Glyceraldehyde-3-phosphate dehydrogenase, activity

Glyceraldehyde-3-phosphate dehydrogenase, muscl

Glyceraldehyde-3-phosphate dehydrogenases and

Heart glyceraldehyde-3-phosphate dehydrogenase

Helix, glyceraldehyde-3-phosphate dehydrogenase

Histidine residues glyceraldehyde-3-phosphate dehydrogenase

Liver glyceraldehyde-3-phosphate dehydrogenase

Muscle glyceraldehyde-3-phosphate .dehydrogenase

NADP-glyceraldehyde-3-phosphate dehydrogenase

Nucleotide binding domain glyceraldehyde phosphate dehydrogenase

Plants glyceraldehyde-3-phosphate dehydrogenases

Protein glyceraldehyde-3-phosphate dehydrogenase

Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Tyrosine residues glyceraldehyde-3-phosphate dehydrogenase

Yeast glyceraldehyde-3-phosphate dehydrogenase

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