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Nicotinamide cofactors

Many dehydrogenase enzymes catalyze oxidation/reduction reactions with the aid of nicotinamide cofactors. The electrochemical oxidation of nicotinamide adeniiw dinucleotide, NADH, has been studied in depthThe direct oxidation of NADH has been used to determine concentration of ethanol i s-isv, i62) lactate 157,160,162,163) pyTuvate 1 ), glucose-6-phosphate lactate dehydrogenase 159,161) alanine The direct oxidation often entails such complications as electrode surface pretreatment, interferences due to electrode operation at very positive potentials, and electrode fouling due to adsorption. Subsequent reaction of the NADH with peroxidase allows quantitation via the well established Clark electrode. [Pg.65]

Human CYPs are multicomponent enzyme systems, requiring at a minimum the CYP enzyme component and a reductase component to be functional. The reductase requires a reduced nicotinamide cofactor, typically NADPH, and this cofactor must be regenerated to provide a steady supply of reducing equivalents for the reductase. Regeneration is accomplished with a separate substrate and enzyme. Glucose-6-phosphate and glucose-6-phosphate dehydrogenase have been widely used for this purpose. The overall complexity of the reaction mixtures and their cost have been barriers to the widespread use of recombinant human CYPs for metabolite synthesis in the past. [Pg.220]

Each reaction was performed with a CYP biocatalyst concentration of 1 pM (1000 nmol L 1), in the presence of a corresponding CYP reaction mix containing reduced nicotinamide cofactor and a cofactor recycling system at 30 °C, with agitation to promote oxygen transfer to the reaction solution. [Pg.221]

Transition Metal-Catalyzed Regeneration of Nicotinamide Cofactors... [Pg.1471]

The most important coenzymes in synthetic organic chemistry [14] and industrially applied biotransformations [15] are the nicotinamide cofactors NAD/ H (3a/8a, Scheme 43.1) and NAD(P)/H (3b/8b, Scheme 43.1). These pyridine nucleotides are essential components of the cell [16]. In all the reactions where they are involved, they serve solely as hydride donors or acceptors. The oxidized and reduced form of the molecules are shown in Scheme 43.1, the redox reaction taking place at the C-4 atom of the nicotinamide moiety. [Pg.1471]

Scheme 43.1 Oxidized (left, NAD(P), 3a/3b) and reduced (right, NAD(P)H, 8a/8b) forms of nicotinamide cofactors. Scheme 43.1 Oxidized (left, NAD(P), 3a/3b) and reduced (right, NAD(P)H, 8a/8b) forms of nicotinamide cofactors.
Fig. 43.2 Costs of nicotinamide cofactors (Source Julich Fine Chemicals, 2003). Fig. 43.2 Costs of nicotinamide cofactors (Source Julich Fine Chemicals, 2003).
A number of photochemically or photoelectrochemically activated transition-metal complexes have also been used, both for oxidation and reduction of the nicotinamide cofactors. Among these complexes is the aforementioned Cp Rh(bpy)-complex 9 [52, 53]. For details of these systems or other regeneration procedures using special dyes, the reader is referred to other reviews on coenzyme regeneration [17, 21-23]. [Pg.1479]

Until now, only a few versatile, selective and effective transition-metal complexes have been applied in nicotinamide cofactor reduction. The TOFs are well within the same order of magnitude for all systems studied, and are within the same range as reported for the hydrogenase enzyme thus, the catalytic efficiency is comparable. The most versatile complex Cp Rh(bpy) (9) stands out due to its acceptance of NAD+ and NADP+, acceptance of various redox equivalents (formate, hydrogen and electrons), and its high selectivity towards enzymatically active 1,4-NAD(P)H. [Pg.1479]

Hydride-transfer reactions involving nicotinamide cofactors 48 Commitments 55... [Pg.28]

HYDItIDE-TItANSFER REACTIONS INVOLVING NICOTINAMIDE COFACTORS... [Pg.49]

The report of Basran et al. (entry 5 of Table 2) contains two studies involving hydride transfer with nicotinamide cofactors. In morphinone-reductase catalyzed reduction by NADH of the flavin cofactor FMN (schematic mechanism in Fig. 5), the primary isotope effects are modest (around 4 for H/D), but exhibit a small value of Ajj/Aq (0.13) and an exalted isotopic difference in energies of activation (8.2kJ/mol) that alone would have generated an isotope effect around 30. The enthalpies of activation are in the range of 35-45 kJ/mol. This is behavior typical of Bell tunneling as discussed above. It can also be reproduced by more complex models, as will be discussed in later parts of this review. [Pg.58]

All bacteria where nitrate ester degradation has been characterized have very similar enzymes. The enzymes eatalyze the nicotinamide cofactor-dependent reductive eleavage of nitrate esters that produces alcohol and nitrite. Purification of the PETN reduetase from Enterobacter cloacae yielded a monomerie protein of around 40 kilo Daltons, which required NADPH as a co-faetor for aetivity. Similar enzymes were responsible for the nitrate ester-degrading activity in Agrobacterium radiobacter (Snape et al. 1997) - nitrate ester reductase - and in the strains of Pseudomonas fluorescens and Pseudomonas putida (Blehert et al. 1999) - xenobiotic reduetases . All utilize a non-covalently bound flavine mononucleotide as a redox eofactor. [Pg.213]

Similar to the AAOs, the aaDHs catalyze oxidative deamination, forming an oxoacid and ammonia. However, rather than using enzyme-hound FAD as the oxidant, followed hy O2, these enzymes employ nicotinamide cofactors, NAD or NADP, in free solution (Equation (3)). [Pg.76]

Biochemical Effects Several enzymes that use nicotinamide cofactors were found to ye inhibited by PAN (at 125 ppm for 1 min) in in vitro studies. These enzymes were most susceptible in the absence of substrates. In some cases, an enzyme was protected by the nicotinamide cofactor (e.g., G-6-PD plus NADP), and in other cases, by the cosubstrate (e.g., isocitrate dehydrogenase plus isocitrate). Precisely the same protection could be obtained when compounds that react with sulfhydryl compounds (e.g., p-mercuricbenzoate) were used instead of PAN. Thus, the evidence indicated that PAN reacted with sulfhydryl groups. [Pg.456]

In the second approach the reducing equivalents are suppHed by a nicotinamide cofactor (NADH or NADPH) and for commercial viability it is necessary to regenerate the cofactor using a sacrificial reductant ]12]. This can be achieved in two ways substrate coupled or enzyme coupled (Scheme 6.2). Substrate-coupled regeneration involves the use of a second alcohol (e.g. isopropanol) that can be accommodated by the KRED in the oxidative mode. A problem with this approach is that it affords an equilibrium mixture of the two alcohols and two ketones. In order to obtain a high yield of the desired alcohol product a large excess of the sacrificial alcohol needs to be added and/or the ketone product (acetone) removed... [Pg.112]

Another approach to preparing enantiomerically pure carboxylic acids and related compounds is via enanhoselective reduction of conjugated double bonds using NAD(P)H-dependent enoate reductases (EREDs EC 1.3.1.X), members of the so-called Old Yellow Enzyme family [44]. EREDs are ubiquitous in nature and their catalytic mechanism is well documented [45]. They contain a catalytic flavin cofactor and a stoichiometric nicotinamide cofactor which must be regenerated (Scheme 6.23). [Pg.125]

Analogous to the KRED reductions they can be performed as whole-cell biotransformations [48, 49] (baker s yeast, for example, contains a number of EREDs) or with isolated enzymes [50-52]. In the latter case the nicotinamide cofactor can... [Pg.125]

Chenault, H.K. and Whitesides, G.M. (1987) Regeneration of nicotinamide cofactors for use in organic synthesis. Appl Biochem Biotechnol, 14, 147-97. [Pg.239]

Ketoreductases (KREDs) are dependent on nicotinamide cofactors NADH or NADPH. Due to the reaction mechanism, these rather costly cofactors are needed in stoichiometric amounts, disclosing an economic problem that has to be dealt with when using these enzymes. Many different possibilities for cofactor recycling have been established with three major approaches finding application in research and industry (Fig. 13). Further regeneration systems, such as electrochemical methods, are not discussed within this review [22-24, 37, 106-108],... [Pg.14]


See other pages where Nicotinamide cofactors is mentioned: [Pg.371]    [Pg.394]    [Pg.229]    [Pg.301]    [Pg.302]    [Pg.302]    [Pg.82]    [Pg.234]    [Pg.471]    [Pg.477]    [Pg.1472]    [Pg.340]    [Pg.69]    [Pg.148]    [Pg.14]    [Pg.14]    [Pg.19]    [Pg.202]    [Pg.157]    [Pg.203]   
See also in sourсe #XX -- [ Pg.13 ]

See also in sourсe #XX -- [ Pg.198 ]

See also in sourсe #XX -- [ Pg.209 , Pg.228 ]




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