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Acetaldehyde pyruvate decarboxylase

In general, pyruvate decarboxylase (EC 4.1.1.1) catalyzes the decarboxylation of a 2-oxocar-boxylic acid to give the corresponding aldehyde6. Using pyruvic acid, the intermediately formed enzyme-substrate complex can add an acetyl unit to acetaldehyde already present in the reaction mixture, to give optically active acetoin (l-hydroxy-2-butanone)4 26. Although the formation of... [Pg.675]

These enzymes catalyse the non-hydrolytic cleavage of bonds in a substrate to remove specific functional groups. Examples include decarboxylases, which remove carboxylic acid groups as carbon dioxide, dehydrases, which remove water, and aldolases. The decarboxylation of pyruvic acid (10.60) to form acetaldehyde (10.61) takes place in the presence of pyruvic decarboxylase (Scheme 10.13), which requires the presence of thiamine pyrophosphate and magnesium ions for activity. [Pg.80]

The requirement for NAD+ is to reoxidize the lipoic acid carrier. It is worth mentioning that the pyruvate acetaldehyde conversion we considered at the end of the glycolytic pathway involves the same initial sequence, and pyruvate decarboxylase is another thiamine diphosphate-dependent enzyme. [Pg.585]

Figure B.l. Mechanism for the conversion of pyruvic acid to acetaldehyde and CO2 by pyruvate decarboxylase. Figure B.l. Mechanism for the conversion of pyruvic acid to acetaldehyde and CO2 by pyruvate decarboxylase.
In the first step, pyruvate is decarboxylated in an irreversible reaction catalyzed by pyruvate decarboxylase. This reaction is a simple decarboxylation and does not involve the net oxidation of pyruvate. Pyruvate decarboxylase requires Mg24" and has a tightly bound coenzyme, thiamine pyrophosphate, discussed below. In the second step, acetaldehyde is reduced to ethanol through the action of alcohol dehydrogenase, with... [Pg.538]

TPP-dependent enzymes catalyze either simple decarboxylation of a-keto acids to yield aldehydes (i.e. replacement of C02 with H+), or oxidative decarboxylation to yield acids or thioesters. The latter type of reaction requires a redox coenzyme as well (see below). The best known example of the former non-oxidative type of decarboxylation is the pyruvate decarboxylase-mediated conversion of pyruvate to acetaldehyde and C02. The accepted pathway for this reaction is shown in Scheme 10 (69MI11002, B-70MI11003, B-77MI11001>. [Pg.267]

Ketols can also be formed enzymatically by cleavage of an aldehyde (step a, Fig. 14-3) followed by condensation with a second aldehyde (step c, in reverse). An enzyme utilizing these steps is transketolase (Eq. 17-15),132b which is essential in the pentose phosphate pathways of metabolism and in photosynthesis. a-Diketones can be cleaved (step d) to a carboxylic acid plus active aldehyde, which can react either via a or c in reverse. These and other combinations of steps are often observed as side reactions of such enzymes as pyruvate decarboxylase. A related thiamin-dependent reaction is that of pyruvate and acetyl-CoA to give the a-diketone, diacetyl, CH3COCOCH3.133 The reaction can be viewed as a displacement of the CoA anion from acetyl-CoA by attack of thiamin-bound active acetaldehyde derived from pyruvate (reverse of step d, Fig. 14-3 with release of CoA). [Pg.736]

EC 1.11.1.7) (68) and diphenol oxidase (EC 1.10.3.1) (69) have been identified. The potential role of pyruvic decarboxylase (EC 4.1.1.1) catalyzed reaction as a source of acetaldehyde and other aldehydes in juice was discussed (70). Raymond et al. (71) isolated the decarboxylase from orange juice sections and demonstrated that only 10 to 15% of the enzyme was in an active form. Since the purified enzyme was only active with pyruvic acid and 2-ketobutyric acid of the series of 2-ketoacids examined, they (71) concluded that the direct contribution of orange pyruvic decarboxylase to the orange volatile profile was limited to acetaldehyde and possibly propionaldehyde. [Pg.162]

Rosche B, Breuer M et al (2004) Biphasic aqueous/organic biotransformation of acetaldehyde and benzaldehyde by Zymomonas mobilis pyruvate decarboxylase. Biotechnol Bioeng 86 788-794... [Pg.44]

Conversion to ethanol. In yeast and some other microorganisms under anaerobic conditions, the NAD+ required for the continuation of glycolysis is regenerated by a process called alcoholic fermentation. The pyruvate is converted to acetaldehyde (by pyruvate decarboxylase) and then to ethanol (by alcohol dehydrogenase), the latter reaction reoxidizing the NADH to NAD+ ... [Pg.284]

The a-keto acid decarboxylases such as pyruvate (E.C. 4.1.1.1) and benzoyl formate (E.C. 4.1.1.7) decarboxylases are a thiamine pyrophosphate (TPP)-dependent group of enzymes, which in addition to nonoxidatively decarboxylating their substrates, catalyze a carboligation reaction forming a C-C bond leading to the formation of a-hydroxy ketones.269-270 The hydroxy ketone (R)-phenylacetylcarbinol (55), a precursor to L-ephedrine (56), has been synthesized with pyruvate decarboxylase (Scheme 19.35). BASF scientists have made mutations in the pyruvate decarboxylase from Zymomonas mobilis to make the enzyme more resistant than the wild-type enzyme to inactivation by acetaldehyde for the preparation of chiral phenylacetylcarbinols.271... [Pg.382]

A number of investigators (15, 16, 17), working with pyruvate decarboxylase, actually isolated the pyruvate adduct to thiamin pyrophosphate, and demonstrated that the enzyme will then decar-boxylate that adduct to yield C02 and acetaldehyde. In an elegant biomimetic study, Lienhard (18, 19) and his collaborators synthesized an analog of this adduct, and showed that it undergoes decarboxylation upon heating in water. Further, the rate is enhanced 105-fold by carry-... [Pg.27]

Calculate the entropy change for the conversion of pyruvic acid (CH3COCOOH) into acetaldehyde and C02 by the enzyme pyruvate decarboxylase at 25°C and 100 atm. [Pg.54]

Yeast, a facultative anaerobe, uses alcoholic fermentation (Sec. 11.2) pyruvate decarboxylase catalyzes the conversion of pyruvate to acetaldehyde, and then alcohol dehydrogenase converts the acetaldehyde to ethyl alcohol and oxidizes NADH to NAD+. [Pg.332]

The identity of the enzyme(s) involved in the latter reaction has been debated (13). However, the formation of the above hydro-xyketone, in analogy with acetoin, has been conceptualized as the consequence of the condensation of the "active" form of acetaldehyde, that is formed by decarboxylative addition of pyruvate to thiamine pyrophospate, with benzaldehyde.The role of pyruvate, in fact has been established. The same mechanism can be invoked for the reaction of cinnamaldehyde.lt is known that the pyruvate decarboxylase (E.C. 4.1.1.1) accepts as substrates a-oxoacids... [Pg.349]

The biogenesis of solerone 1 and related compounds was successfully rationalized by biomimetic model reactions. As key step we established the pyruvate decarboxylase catalyzed acyloin condensation of pyruvic acid with ethyl 4-oxobutanoate 4 or ethyl 2-oxoglutarate 3 with acetaldehyde. The importance of the ethyl ester function in 3 and 4 serving as substrates for the enzymatic formation of a-hydroxy ketones 5 and 6 was demonstrated. The identification of six yet unknown sherry compounds including acyloins 5 and 6, which have been synthesized for the first time, confirmed the relevance of the biosynthetic pathway. Application of MDGC-MS allowed the enantiodifferentiation of a-ketols and related lactones in complex sherry samples and disclosed details of their biogenetic relationship. [Pg.122]

Unfortunately diacetyl formation is still not well understood. Acetoin formation occurs either by nonspecific interaction of acetaldehyde with the a-hydroxyethyl thiamine pyrophosphate intermediate in pyruvate decarboxylation (209) or by decarboxylation of a-acetolactate (210), which in turn arises either from interaction of pyruvate with a-hydroxyethyl thiamine pyrophosphate (211) or as a specific intermediate in valine biosynthesis (212, 213). Diacetyl does not appear to be formed directly from acetoin (208, 214). It is formed from a-acetolactate, in absence of cells, by O2 oxidation (215), and even under N2 (216), although an oxidation must occur. It is also formed from acetyl CoA (217, 218), probably by interaction with a-hydroxyethyl thiamine pyrophosphate [cf. stimulation by acetyl CoA addition to a solution of pyruvate and pyruvate decarboxylase (2i5)]. It is not known whether this involves a specific enzyme or is a mere side reaction. [Pg.260]


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See also in sourсe #XX -- [ Pg.302 ]

See also in sourсe #XX -- [ Pg.302 ]

See also in sourсe #XX -- [ Pg.302 ]

See also in sourсe #XX -- [ Pg.302 ]




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Pyruvate decarboxylase

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