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Keto acids enzymic reductions

The investigation of the aminotransferase activity of apple ACS carried out by Feng et al reveals that it is able to reductively aminate PLP to PMP by transamination of some L-amino acids to their corresponding a-keto acids. The enzyme has shown substrate specificity with the preference of Ala > Arg > Phe > Asp. The addition of excess pyruvate causes a conversion of the PMP form of the enzyme back to the PLP form. The quite unstable PMP form of ACS can generate apoenzyme, which captures PLP to restore its physiologically active form. [Pg.96]

This enzyme [EC 1.4.99.1] catalyzes the oxidation-reduction reaction of a D-amino acid with an acceptor and water to generate an a-keto acid, ammonia, and the reduced acceptor. The enzyme utilizes FAD as a cofactor. Most D-amino acids, with the noted exceptions of D-aspartate and D-glutamate, can be used as substrates. K. Tsukada (1971) Meth. Enzymol. 17B, 623. [Pg.53]

An elegant four-enzyme cascade process was described by Nakajima et al. [28] for the deracemization of an a-amino acid (Scheme 6.13). It involved amine oxidase-catalyzed, (i )-selective oxidation of the amino acid to afford the ammonium salt of the a-keto acid and the unreacted (S)-enantiomer of the substrate. The keto acid then undergoes reductive amination, catalyzed by leucine dehydrogenase, to afford the (S)-amino acid. NADH cofactor regeneration is achieved with formate/FDH. The overall process affords the (S)-enantiomer in 95% yield and 99% e.e. from racemic starting material, formate and molecular oxygen, and the help of three enzymes in concert. A fourth enzyme, catalase, is added to decompose the hydrogen peroxide formed in the first step which otherwise would have a detrimental effect on the enzymes. [Pg.119]

R)-2-Hydroxy-4-phenylbutyric acid was produced continuously in an enzyme membrane reactor by enzymatic reductive animation of the a-keto acid with d-lactate dehydrogenase coupled with formate dehydrogenase (FDH) for regeneration of NADH. Reactor performance data matched a kinetic reactor model (Schmidt, 1992). [Pg.554]

For fatty acid biosynthesis, reduction after each condensation step affords a growing hydrocarbon chain. In the absence of this reduction process, the growing poly- -keto chain needs to be stabilized on the enzyme surface until the chain length is complete, at which point cyclization or other reactions can occur. The poly-fj-kelo ester is very reactive, and there are various possibilities... [Pg.60]

Enzyme-catalyzed syntheses of enantiomeric pure hydroxy acids use lactate dehydrogenases (LDH E.C. 1.1.1.27) or hydroxyisocaproate dehydrogenases (HicDH). Both kinds of enzymes are available as D- or L-specific catalysts. L-specific [5, 6] LDHs as well as D-specific [7-10] LDHs favorably catalyze the reduction of pyruvate, HicDHs (and mandelate dehydrogenase, too) convert keto acids with longer aliphatic or aromatic side chains. These enzymes can be isolated from Lactobacillus strains [11-14]. [Pg.147]

Reductive amination reactions of keto acids are performed with amino acid dehydrogenases. NAD-dependent leucine dehydrogenase from Bacillus sp. is of interest for the synthesis of (S)-fert.-leucine [15-17]]. This chiral compound has found widespread application in asymmetric synthesis and as a building block of biologically active substances. The enzyme can also be used for the chemoenzy-matic preparation of (S)-hydroxy-valine [18] and unnatural hydrophobic bran-ched-chain (S)-amino acids. NAD-dependent L-phenylalanine dehydrogenase from Rhodococcus sp. [19] has been used for the synthesis of L-homophenyl-alanine ((S)-2-Amino-4-phenylbutanoic acid) [9]. These processes with water-soluble substrates and products demonstrate that the use of coenzymes must not... [Pg.147]

Lactones are cyclic compounds formed through the intramolecular esterification of a hydroxy fatty acid. 7-Lactones and 8-lactones, with fivesided and six-sided rings, respectively have been found in cheese (Jolly and Kosikowski, 1975 Wong et al., 1975 Collins et al., 2004). The origin of the precursor hydroxy fatty acids has been ascribed to a 8-oxidation system in the mammary gland of ruminants (see Fox et al., 2000), the reduction of keto acids (Wong et al., 1975) and/or the action of lipoxygenases and other enzymes present in members of the rumen microflora (Dufosse et al., 1994). Lactones have low flavor thresholds and while their aromas are not specifically cheese-like (their aromas have been described variously as peach, apricot and coconut ), they may contribute to the overall flavor of cheese (see Collins et al., 2004). [Pg.410]

Enzymatic synthesis of E-tm-leucine is another example of the use of isolated enzymes (Bommarius et al, 1995). An NADH-dependent leucine dehydrogenase was used as a catalyst for the reductive amination of the corresponding keto acid together with formate dehydrogenase (FDH) and formate as a cofactor regenerator (Fig. 19.5b Shaked and Whitesides, 1980 Wichmann et al, 1981). Furthermore, a unique membrane reactor system involving FDH and PEG-modihed-NAD for continuous NADH regeneration... [Pg.363]

Fig. 8 Synthesis of amino acids by a multienzyme system consisting of leucine dehydrogenase (LeuDH) catalyzing the reductive amination of the corresponding keto acid, L-lactate dehydrogenase (l-LDH), and lactate for the regeneration of NADH and urease for the in situ generation of ammonia. The coenzyme NAD+ was covalently bond to dextran, enzymes and dextran-coupled NAD+ were... Fig. 8 Synthesis of amino acids by a multienzyme system consisting of leucine dehydrogenase (LeuDH) catalyzing the reductive amination of the corresponding keto acid, L-lactate dehydrogenase (l-LDH), and lactate for the regeneration of NADH and urease for the in situ generation of ammonia. The coenzyme NAD+ was covalently bond to dextran, enzymes and dextran-coupled NAD+ were...
L-Lactate dehydrogenase (l-LDH, EC 1.1.1.27) catalyzes the reduction of pyruvate to (S)-lactate with a simultaneous oxidation of NADH. l-LDH is found in all higher organisms. There are two kinds of l-LDHs enzymes from one group are activated by fructose 1,6-diphosphate while the other group stays independent [71]. l-LDH is highly selective for pyruvate, short-chain 2-keto acids and phenylpyruvic acid [80]. All bacterial NAD+-dependent LDHs form lactate from pyruvate in vivo, and there is no evidence at all that they catalyze the other direction as well. The equilibrium constant lies far on the direction of lactate formation, and thus the reaction catalyzed by bacterial LDHs can be considered almost irreversible. LDHs from some lacto-bacilli like Lactobacillus fermentum or L. cellobiosus show no or just poor reaction with lactate [71], whereas mammalian LDHs can be considered as reversible [71]. Well characterized l-LDHs are summarized in Table 2. [Pg.208]

The coupling of these two enzymatic systems could find many more applications due to the avaUabihty of amino acid dehydrogenases of broader specificity [31]. A series of amino acid dehydrogenases with D-specificity for the preparation of D-amino acids has been applied to the reductive amination of a-keto acids [32]. However, the deracemization of rac-amino acids exploiting this type of enzyme requires an amino acid oxidase with L-specificily, which is a rare enzymatic activity. As an alternative the a-oxo acid, usually available through difficult synthetic procedures, can be used directly. [Pg.204]

DAAO is one of the most extensively studied flavoprotein oxidases. The homodimeric enzyme catalyzes the strictly stere-ospecihc oxidative deamination of neutral and hydrophobic D-amino acids to give a-keto acids and ammonia (Fig. 3a). In the reductive half-reaction the D-amino acid substrate is converted to the imino acid product via hydride transfer (21). During the oxidative half-reaction, the imino acid is released and hydrolyzed. Mammalian and yeast DAAO share the same catalytic mechanism, but they differ in kinetic mechanism, catalytic efficiency, substrate specificity, and protein stability. The dimeric structures of the mammalian enzymes show a head-to-head mode of monomer-monomer interaction, which is different from the head-to-tail mode of dimerization observed in Rhodotorula gracilis DAAO (20). Benzoate is a potent competitive inhibitor of mammalian DAAO. Binding of this ligand strengthens the apoenzyme-flavin interaction and increases the conformational stability of the porcine enzyme. [Pg.506]

Many mononuclear nonheme iron oxygenases require a reducing cofactor (pterin or alpha-keto acid) for dioxygen activation.23,128 These enzymes utilize Fe(I V) > Fe (II) reduction by two-electron substrates. A simplified catalytic cycle for 2-keto-glutarate-dependent enzymes is shown in Figure 4.34. Keto-glutarate cofactors assist... [Pg.166]

FDH from Candida boidinii is mostly used as regeneration enzyme. It found industrial application at Degussa-Hiils AG in a leucine dehydrogenase-catalyzed reductive animation of 2-keto acids yielding various amino acids (e.g. tert-leu-cine) l14-16l. Native FDH is very selective for NAD+. Recently a new FDH was developed by site-directed mutagenesis that shows all advantages of the NAD+-dependent enzymes and additionally accepts NADP+ as substrate1171. The activity of the mutant with NADP+ is about 60% of the wild-type FDH with NAD+[18 . [Pg.1247]


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Reductive enzymes

Reductive keto acids

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