EC Number | Application | Comment | Organism |
---|---|---|---|
4.1.1.1 | synthesis | engineered enzyme mutants are useful for synthesis of both enantiomers of alpha-ketols and acetolactates with good enantiomeric excess, overview | Saccharomyces cerevisiae |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.1 | expression of mutants D28A and His6-tagged E477Q | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.1 | D28A | site-directed mutagenesis, the mutant enzyme shows additional carboligation activity | Saccharomyces cerevisiae |
4.1.1.1 | E477Q | site-directed mutagenesis, the mutant enzyme shows additional carboligation activity | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.1 | additional information | - |
additional information | steady-state kinetic parameters for beta-hydroxypyruvate | Saccharomyces cerevisiae |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.1 | Mg2+ | required for activity | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.1 | a 2-oxo acid | Saccharomyces cerevisiae | - |
an aldehyde + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.1 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.1 | recombinant mutants D28A and His6-tagged E477Q, the latter on a talon resin | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.1 | 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 | - |
? | |
4.1.1.1 | a 2-oxo acid | - |
Saccharomyces cerevisiae | an aldehyde + CO2 | - |
? | |
4.1.1.1 | beta-hydroxypyruvate | D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor | Saccharomyces cerevisiae | 2,4-dihydroxymethyl-3-oxo-butanoic acid | - |
? | |
4.1.1.1 | beta-hydroxypyruvate | - |
Saccharomyces cerevisiae | glycolaldehyde + ? | - |
? | |
4.1.1.1 | 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 | - |
? | |
4.1.1.1 | 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 | ? | - |
? | |
4.1.1.1 | 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 | ? | |
4.1.1.1 | 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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.1 | yeast pyruvate decarboxylase | - |
Saccharomyces cerevisiae |
4.1.1.1 | YPDC | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.1 | 30 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.1 | 6 | - |
- |
Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.1 | thiamine diphosphate | dependent on | Saccharomyces cerevisiae |