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Literature summary for 4.1.1.1 extracted from

  • Baykal, A.; Chakraborty, S.; Dodoo, A.; Jordan, F.
    Synthesis with good enantiomeric excess of both enantiomers of alpha-ketols and acetolactates by two thiamine diphosphate-dependent decarboxylases (2006), Bioorg. Chem., 34, 380-393.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.1

Application

Application Comment Organism
synthesis engineered enzyme mutants are useful for synthesis of both enantiomers of alpha-ketols and acetolactates with good enantiomeric excess, overview Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutants D28A and His6-tagged E477Q Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D28A site-directed mutagenesis, the mutant enzyme shows additional carboligation activity Saccharomyces cerevisiae
E477Q site-directed mutagenesis, the mutant enzyme shows additional carboligation activity Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetic parameters for beta-hydroxypyruvate Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a 2-oxo acid Saccharomyces cerevisiae
-
 an aldehyde + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mutants D28A and His6-tagged E477Q, the latter on a talon resin Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 pyruvate D28A YPDC variant, not E477Q YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview Saccharomyces cerevisiae (S)-acetolactate + CO2
-
 ?
a 2-oxo acid
-
 Saccharomyces cerevisiae an aldehyde + CO2
-
 ?
beta-hydroxypyruvate D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor Saccharomyces cerevisiae 2,4-dihydroxymethyl-3-oxo-butanoic acid
-
 ?
beta-hydroxypyruvate
-
 Saccharomyces cerevisiae glycolaldehyde + ?
-
 ?
beta-hydroxypyruvate + glycolaldehyde E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor Saccharomyces cerevisiae 1,3,4-trihydroxy-2-butanone
-
 ?
additional information thiamine-dependent decarboxylases/dehydrogenases can also carry out socalled carboligation reactions, where the central ThDP-bound enamine intermediate reacts with electrophilic substrates, YPDC can produce acetoin and acetolactate, resulting from the reaction of the central thiamine diphosphate-bound enamine with acetaldehyde and pyruvate, respectively, overview, analysis of the stereoselectivity for forming the carboligase products acetoin, acetolactate, and phenylacetylcarbinol by the YPDC mutants E477Q and D28A Saccharomyces cerevisiae ?
-
 ?
pyruvate + acetaldehyde E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor Saccharomyces cerevisiae acetoin + CO2 i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers ?
pyruvate + benzaldehyde E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview Saccharomyces cerevisiae (R)-phenylacetylcarbinol + CO2
-
 ?

Synonyms

Synonyms Comment Organism
yeast pyruvate decarboxylase
-
 Saccharomyces cerevisiae
YPDC
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent on Saccharomyces cerevisiae