Hefecarboxylase und die Bildung von Phenylacetylcarbinol

Hanc, O; Kakáč, B.

doi:10.1007/bf00632526

Cited by 19 publications

(7 citation statements)

References 1 publication

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“…Carboligases have appeared in a number of reports,3 "-'10) and among them PDH, which catalyzes pyruvate-glyoxylate carboligase reaction,4) and pyruvate decarboxylase, which catalyzes acetylphenylcarbinol 6 ) and N-phenylacetohydroxamic acid 7 ) formationsresemble DKS~Iin that the substrate is pyruvate. Therefore, we examined whether the purified preparations of E. coli PDH and bovine heart PDC catalyze the carboligasereaction between pyruvate and aldoses to form I-deoxy-ketoses (DKS-I activity).…”

Section: Dks-i Activity In the Purified Preparations Of E Coli Pdh Amentioning

confidence: 99%

Formation of 1-Deoxy-ketoses by Pyruvate Dehydrogenase and Acetoin Dehydrogenase

Yokota

Sasajima²

1986

Agricultural and Biological Chemistry

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Section: Dks-i Activity In the Purified Preparations Of E Coli Pdh Amentioning

confidence: 99%

Formation of 1-Deoxy-ketoses by Pyruvate Dehydrogenase and Acetoin Dehydrogenase

Yokota

Sasajima²

1986

Agricultural and Biological Chemistry

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“…2-0x0 acid carboxylyase, pyruvate decarboxylase), and requires thiamin as a cofactor (31,32). The course of the reaction (Scheme 3) is evidently analogous to that of the carboxylasecatalyzed formation of acetoin from acetaldehyde and pyruvate (36)(37)(38).…”

Section: Discussionmentioning

confidence: 98%

“…The latter compound has been reported to be the major product when yeast (Saccharomyces cerevisiae) is incubated with benzaldehyde (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35) in the presence of fermentable sugars (25,27,30,(33)(34)(35), pyruvic acid (25,29,31,32), or acetyl phosphate (3 1). The relative amounts of (S)-and (R)-1-hydroxy-1-phenyl-2-propanone that are formed are determined by the stereoselectivity of this reaction.…”

Section: Discussionmentioning

confidence: 99%

The biosynthesis of ephedrine

Grue-Sørensen¹,

Spenser²

1989

Can. J. Chem.

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It is shown by 13C nuclear magnetic resonance spectroscopy that the labelled C2 fragment of [2,3-13C2]pyruvic acid is transferred intact into the C-methyl group and the adjacent carbon atom of the Ephedra alkaloids, norephedrine, ephedrine, norpseudoephedrine, and pseudoephedrine, in growing plants of Ephedragerardiana. This finding serves to identify pyruvate as the elusive precursor of the aliphatic C2 terminus of the skeleton of the alkaloids. In earlier experiments with C-labelled substrates, label from [3-14C]pyruvic acid was incorporated mainly, but not exclusively, into the C-methyl group of ephedrine, and label from [2-14C]pyruvate was incorporated similarly into the carbon atom adjacent to the C-methyl group. A C6–C1 unit related to benzaldehyde or benzoic acid has long been known to generate the benzylic fragment of the carbon skeleton of the Ephedra alkaloids. It is likely that the carbon skeleton of ephedrine is generated from pyruvate and either benzaldehyde or benzoic acid, by a reaction analogous to the formation of acetoin or diacetyl from pyruvate and acetaldehyde or acetic acid, respectively. Keywords: biosynthesis of ephedrine, Ephedra alkaloids, 13C NMR spectra, ephedrine, biosynthesis of pyruvic acid, incorporation into ephedrine13C NMR spectra.

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“…The manufacture of R-PAC is currently based on a fermentation process in which yeast cells carry out the enzymatic condensation of pyruvate with externally supplied benzaldehyde (Hildebrandt and Klavehn, 1932;Rogers et al, 1997). The action of yeast pyruvate decarboxylase (PDC) is responsible for this transformation (Hanc and Karac, 1956). The enzyme catalyzes the thiamin diphosphate (ThDP)-dependent decarboxylation of the a-keto acid pyruvate to acetaldehyde as its physiologically significant reaction but can catalyze condensation (carboligation) of pyruvate with aldehydes to form a-hydroxy ketones as a side reaction (Iding et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of α‐hydroxy ketones

Engel

Vyazmensky

Berkovich

et al. 2004

Biotech & Bioengineering

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Acetohydroxy acid synthase I appears to be the most effective of the AHAS isozymes found in Escherichia coli in the chiral synthesis of phenylacetyl carbinol from pyruvate and benzaldehyde. We report here the exploration of a range of aldehydes as substrates for AHAS I and demonstrate that the enzyme can accept a wide variety of substituted benzaldehydes, as well as heterocyclic and heteroatomic aromatic aldehydes, to produce chiral carbinols. The active site of AHAS I does not appear to impose serious steric constraints on the acceptor substrate. The influence of electronic effects on the reaction has been probed using substituted benzaldehydes as substrates. The electrophilicity of the aldehyde acceptor substrates is most important to their reactivity, but the lipophilicity of substituents also affects their reactivity. AHAS I is an effective biosynthetic platform for production of a variety of alpha-hydroxy ketones, compounds with considerable potential as pharmacological precursors.

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Hefecarboxylase und die Bildung von Phenylacetylcarbinol

Cited by 19 publications

References 1 publication

Formation of 1-Deoxy-ketoses by Pyruvate Dehydrogenase and Acetoin Dehydrogenase

Formation of 1-Deoxy-ketoses by Pyruvate Dehydrogenase and Acetoin Dehydrogenase

The biosynthesis of ephedrine

Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of α‐hydroxy ketones

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