NADH-dependent dehydrogenase

It is also a precursor for synthesis of polyprenyl (isoprenoid) compounds, and it can give rise to free acetoacetate, an important constituent of blood. Acetoacetate is a (3-oxoacid that can undergo decarboxylation to acetone or can be reduced by an NADH-dependent dehydrogenase to D-3-hydroxybutyrate. Notice that the configuration of this compound is opposite to that of L-3-hydroxybutyryl-CoA which is... 

No recycling with phosphatase and NAD/NADH dependent dehydrogenase. 

An Approach to Understanding the Stereospecificity of NAD+/NADH-Dependent Dehydrogenases, J. Am. Chem. Soc. 113, 2353-2358. 

Many enzyme-catalyzed reactions involve two or more substrates and enzyme complexes and hence they deviate from the Michaelis-Menten treatment. A direct simplification of this situation consists of keeping one substrate at nonlimiting concentration. For instance, reactions with NAD /NADH dependent dehydrogenases or oxidases using molecular oxygen as electron donor can be readily... 

Insecticide, inhibits the NADH-dependent dehydrogenase in the respiratory chain... 

Scheme 15.4 TK assay based on NADH-dependent dehydrogenase as auxiliary enzyme.

FIGURE 33.2. Active site of a NADH dependent dehydrogenase transferring a hydride between the substrate and the coenzyme. 

Inoue, K., Makino, Y. and Itoh, N. (2005) Production of (A l-chiral alcohols by a hydrogen-transfer bioreduction with NADH-dependent Leifsonia alcohol dehydrogenase (LSADH). Tetrahedron Asymmetry, 16 (15), 2539-2549. 

Fig. 1. The metabolic cycle for the synthesis and degradation of poly(3HB). (1) 3-ketothiolase (2) NADPH-dependent acetoacetyl-CoA reductase (3) poly(3HB) synthase (4) NADH-dependent acetoacetyl-CoA reductase (5), (6) enolases (7) depolymerase (8) d-(-)-3-hydroxybutyrate dehydrogenase (9) acetoacetyl-CoA synthetase (10) succinyl-CoA transferase (11) citrate synthase (12) see Sect. 3...

Rhin(bpy)3]3+ and its derivatives are able to reduce selectively NAD+ to 1,4-NADH in aqueous buffer.48-50 It is likely that a rhodium-hydride intermediate, e.g., [Rhni(bpy)2(H20)(H)]2+, acts as a hydride transfer agent in this catalytic process. This system has been coupled internally to the enzymatic reduction of carbonyl compounds using an alcohol dehydrogenase (HLADH) as an NADH-dependent enzyme (Scheme 4). The [Rhin(bpy)3]3+ derivative containing 2,2 -bipyridine-5-sulfonic acid as ligand gave the best results in terms of turnover number (46 turnovers for the metal catalyst, 101 for the cofactor), but was handicapped by slow reaction kinetics, with a maximum of five turnovers per day.50... 

The successful synthetic application of this electroenzymatic system has first been shown for the in-situ electroenzymatic reduction of pyruvate to D-lactate using the NADH-dependent D-lactate dehydrogenase. Electrolysis at — 0.6 V vs a Ag/AgCl-reference electrode of 50 mL of a 0.1 M tris-HCL buffer of pH 7.5 containing pentamethylcyclopentadienyl-2,2 -bipyridinechloro-rhodium(III) (1 x 10 3 M), NAD+ (2 x 10 3 M), pyruvate (2 x 10 2 M), 1300 units D-lactate dehydrogenase (divided cell, carbon foil electrode) after 3 h resulted in the formation of D-lactate (1.4 x 10 2 M) with an enantiomeric excess of 93.5%. This means that the reaction occurred at a rate of 5 turnovers per hour with respect to the mediator with a 70% turnover of the starting material. The current efficiency was 67% [67],... 

Recently, we adopted the same system for the reduction of 4-phenyl-2-butanone to (S)-4-phenyl-2-butanol using the NADH-dependent horse liver alcohol dehydrogenase (HLADH) and S-ADH from Rhodococcus sp [68] with high enantioselectivity (Fig. 17) [69]. As mediator, we applied the low-molecular... 

An example of coenzyme regeneration with isolated enzymes is L-alanine production from pyruvate with an NADH-dependent alanine dehydrogenase (AlaDH) ... 

A regeneration reaction for NADH that may be used is the conversion of pyravate with a NADH-dependent lactate dehydrogenase (LDH) ... 

You have isolated a tetrameric NAD+-dependent dehydrogenase. You incubate this enzyme with iodo-acetamide in the absence or presence of NADH (at 10 times the Km concentration), and you periodically remove aliquots of the enzyme for activity measurements and amino acid composition analysis. The results of the analyses are shown in the table. 

Under anaerobic conditions, E. coli synthesizes an NADH-dependent fumarate reductase rather than succinate dehydrogenase, the flavoprotein that oxidizes succinate to fumarate. 

Rao, A.V.S. and T. Ramasarma. 2000. NADH-dependent decavanadate reductase, an alternative activity of NADP-specihc isocitrate dehydrogenase protein. Biochim. Biophys. Acta 1474 321-330. 

By replacing the NADH-dependent glutamate dehydrogenase, which is the major nitrogen assimilation route in S. cerevisiae, the NADH formation associated with biomass synthesis was reduced, i. e., the stoichiometric coefficient a in Fig. 1 was reduced. 

Nearly all NAD+-dependent dehydrogenases studied follow an ordered bisubstrate mechanism. In this mechanism, the oxidation of a substrate proceeds in a sequential manner first, NAD+ binds in the active site of the dehydrogenase then the substrate binds next a hydride equivalent is transferred in a chemical step from the bound substrate to the bound NAD+, hence, oxidising the substrate and reducing the NAD+ to NADH the oxidised substrate is then released from the active site and is finally followed by the NADH. 

Glucose is converted to dihydroxyacetone phosphate in glycolysis (Chap. 10), which is then reduced to glycerol 3-phosphate by NADH-dependent glycerol-3-phosphate dehydrogenase. 

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