Dehydrogenases triosephosphate dehydrogenase

NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Triosephosphate dehydrogenase. GAPDH. 

The differential expression of paired cancerous and non-cancerous tissues was visually compared, and 11 spots were up-regulated in cancerous tissues alpha-enolase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) 2 (spots), triosephosphate isomerase, transgelin, calmodulin, MnSOD, PDI A3, cyclophilinA, GST-P, and apolipoprotein A-I precursor (23). 

Z F6P + ATP + 2 NADH + H+ <-> 2 glycerol-3-phosphate + ADP + 2 NAD+ where F6P is fructose-6-phosphate, FDP is fructose-1,6-diphosphate, DHA-P is dihydroxyacetone phosphate, TIM is triosephosphate isomerase, and GDH is glycerol-3-phosphate dehydrogenase. The oxidation of NADH is a measure of the 6-PFK activity and is determined photometrically (decrease of OD per minute) [4]. 

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. 

RNS, ribonuclease LZM, lysozyme SNS, staphylococcal nuclease LZ4, T4 lysozyme PAP, papain TLS, thermolysin, TRX, thioiedoxin FLN, flavodoxin ADH, alcohol dehydrogenase coenzyme domain AKN, adenyl kinase MDG, malate dehydrogenase TIM, triosephosphate isomerase SUB, subtilisin CPA, carboxypeptidase LDH, lactate dehydrogenase PGK, phosphoglycerate kinase GPD, glyceraldehyde 3-phosphate dehydrogenase, HKN, hexokinase. 

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

T. aquaticus, and comparison of this sequence with that of the lobster muscle enzyme shows a sequence identity of 50% which is again significantly higher than was found in comparison of bacterial and liver alcohol dehydrogenase (33) or bacterial and muscle triosephosphate isomerase (SP). 

Eukaryotic peptide chain elongation factor-2 Triosephosphate isomerase Myo-inositol-phosphate synthase Mannose-1-phosphate guanylj transferase Alcohol dehydrogenase Aldehyde reductase Ade5... 

Vajda S, Camacho CJ. Protein-protein docking is the glass half-full or half-empty Trends Biotechnol. 2004 22 110-116. Derreumaux P, Schlick T. The loop opening/closing motion of the enzyme triosephosphate isomerase. Biophys. J. 1998 74 72-81. Gerstein M, Chothia C. Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase. J. Mol Biol 1991 220 133-149. 

A period in the United States in 1939 as a Rockefeller Fellow in the Harvard laboratory of E. J. Cohn widened his experience of proteins and knowledge of their physical chemistry and led to his first crystallization of a muscle jirotein, a myogen from rabbit muscle which was later shown hy other workers to be identical with triosephosphate dehydrogenase. 

Spectrophotometric assay (BIO, L7, S29) is accomplished by a similar incubation, without hydrazine, where excess added triosephosphate isomerase converts triose phosphate formed to DAP, in turn removed as glycerophosphate by reduced nicotinamide-adenine dinucleotide (NADH2, formerly termed DPNH) and added glycerophosphate dehydrogenase. 

All assay methods are based on the forward ALD-catalyzed reaction. Both photometric fixed-time and continuous-monitoring procedures have been developed. In the analytical approach on which all the commonly used procedures and kits are based, the ALD reaction is coupled with two other enzyme reactions. Triosephosphate isomerase (EC 5.3.1.1) is added to ensure rapid conversion of all GLAP to DAP. Glycerol-3-phosphate dehydrogenase (EC 1.1.1.8) is added to reduce the DAP to glycerol-3-phosphate, with NADH acting as hydrogen donor. The decrease in NADH concentration is then measured. 

Triosephosphate Isomerase Glyceradehyde-3-Phosphate Dehydrogenase Phosphoglycerate Kinase Phosphoglycerate Mutase Enolase... 

A number of studies on the metabolism of 3FG and 4FG in Locusta miaratoria have been undertaken. Both 3FG and 4FG are toxic to locust with LD50 s of 4.8 mg/g and 0.6 mg/g respectively. In vitro studies showed that 3FG is metabolized in the fat body, via the NADP-linked aldose reductase, to 3-deoxy-3-fluoro-D-glucitol (3FGL). This metabolite was detected in the hemolymph of the insect and shown to be both a competitive inhibitor and a substrate for NAD-linked sorbitol dehydrogenase, thereby generating 3-deoxy-3-fluoro-D-fructose (3FF) (541. Subsequently, it was shown by in vivo radio-respirometric analysis of C02 and appropriate chase experiments, that 3FG metabolism irreversibly inhibits glycolysis and not the hexose monophosphate shunt or tricarboxylic acid cycle (55). In addition, the release of fluoride ion and H20 from D-[3- H]-3FG was also observed. Based on the mechanism of aldolase (55) and triosephosphate isomerase... 

---