4.1.1.1: pyruvate decarboxylase
This is an abbreviated version!
For detailed information about pyruvate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.1
-
4.1.1.1
-
dendritic
-
plasmacytoid
-
toll-like
-
thiamin
-
claim
-
autoimmune
-
prescript
-
ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
-
zymomonas
-
branched-chain
-
cdc
-
acetaldehyde
-
mobilis
-
sulfonylurea
-
real-world
-
tregs
-
adhes
-
interferon-alpha
-
insurance
-
lupus
-
antigen-presenting
-
statin
-
costimulatory
-
lipoylated
-
erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
-
dabigatran
-
acetolactate
-
marketscan
-
dispensing
-
synthesis
-
hla-dr
-
antimitochondrial
-
acetoin
-
dihydrolipoyl
-
biotechnology
-
pharmacist
-
herbicide-resistant
-
beneficiaries
-
icd-9-cm
-
dihydrolipoamide
-
transacetylase
-
rivaroxaban
-
dichloroacetate
-
enrollees
-
lipoate
- 4.1.1.1
- dendritic
-
plasmacytoid
-
toll-like
- thiamin
-
claim
- autoimmune
-
prescript
- ifn-alpha
-
pharmacy
-
lymphoid
-
herbicide
- zymomonas
-
branched-chain
- cdc
- acetaldehyde
- mobilis
- sulfonylurea
-
real-world
-
tregs
-
adhes
- interferon-alpha
-
insurance
-
lupus
-
antigen-presenting
- statin
-
costimulatory
-
lipoylated
- erythematosus
-
nonadherence
-
refill
-
medicare
-
tolerogenic
- dabigatran
- acetolactate
-
marketscan
-
dispensing
- synthesis
-
hla-dr
-
antimitochondrial
- acetoin
-
dihydrolipoyl
- biotechnology
-
pharmacist
-
herbicide-resistant
-
beneficiaries
-
icd-9-cm
- dihydrolipoamide
- transacetylase
- rivaroxaban
- dichloroacetate
-
enrollees
- lipoate
Reaction
Synonyms
2-oxo acid carboxylyase, 8-10 nm cytoplasmic filament-associated protein, acetohydroxyacid synthase, AHAS, alpha-Carboxylase, alpha-Keto acid carboxylase, ANC27, bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase, Decarboxylase, pyruvate, GPDC1, IFPL730, KivD, KlPDC, KviD, NcPDC, P59NC, PDC, PDC I, PDC II, PDC1, Pdc1p, PDC2, PDC3, PDC4, Pdc5, Pdc5p, Pdc6, PDCS.c., PDCZ.m., PDHC, POR, pyruvamide-activated yeast pyruvate decarboxylase, pyruvate decarboxylase, pyruvate decarboxylase 1, pyruvate decarboxylase 2, pyruvate decarboxylase complex, Pyruvic decarboxylase, R-selective pyruvate decarboxylase, SCPDC, scpdc1, ScPDC5, TTHA1213, yeast pyruvate decarboxylase, YPDC, ZbPDC, ZmPDC
ECTree
4.1.1.1 pyruvate decarboxylaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.1.1.1 - pyruvate decarboxylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-4-methylpentanoate
3-methylbutanaldehyde + CO2
-
-
-
?
2-oxohexanoic acid
pentanal + CO2
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
2-oxomethylvalerate
?
16.7% of the activity with 2-oxoisovalerate
-
-
?
2-oxopentanoate
butanaldehyde + CO2
-
-
-
?
2-oxopentanoic acid
butanal + CO2
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
3-(1H-indol-3-yl)-2-oxopropanoic acid
1H-indol-3-ylacetaldehyde + CO2
-
-
-
-
?
3-phenylpyruvate
2-phenylethanal + CO2
8.8% of the activity with 2-oxoisovalerate
-
-
?
4-methylthio-2-oxobutanoate
3-methylthiopropanal + CO2
7.2% of the activity with 2-oxoisovalerate
-
-
?
benzaldehyde + acetaldehyde
(R)-phenylacetylcarbinol
-
-
reaction proceeds under in vitro assay conditions, colorimetric assay based on reaction
-
?
benzaldehyde + pyruvate
(R)-phenylacetylcarbinol + CO2
-
-
transformation is enhanced by maintenance of neutral pH-value
-
?
benzoylformate
benzaldehyde + CO2
substrate only for mutant mutant I472A
-
-
?
beta-hydroxypyruvate
2,4-dihydroxymethyl-3-oxo-butanoic acid
-
D28A YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
beta-hydroxypyruvate + glycolaldehyde
1,3,4-trihydroxy-2-butanone
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
-
-
?
indole-3-pyruvate
2-(indol-3-yl)-ethanal + CO2
0.1% of the activity with 2-oxoisovalerate
-
-
?
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
pyruvate + phenylacetaldehyde
3-hydroxy-4-phenyl-butan-2-one + CO2
enzyme catalyzes a carboligation as side reaction
-
?
pyruvic acid
acetaldehyde + CO2
-
the structural basis for KdcA, a branched chain 2-keto acid decarboxylase, EC 4.1.1.72, substrate recognition involving residues Ser286, Phe381, Val461 and Met358 of the substrate binding pocket, mutation of Ser286 and Phe381 converts the enzyme to a pyruvate decarboxylase, homology modeling, overview
-
-
?
2 pyruvate
(S)-acetolactate + CO2
-
D28A YPDC variant, not E477Q YPDC variant, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
2-oxobutanoate
propionaldehyde + CO2
-
-
-
?
2-oxoisocaproate
3-methylbutanal + CO2
22.7% of the activity with 2-oxoisovalerate
-
-
?
3-Fluoropyruvate
acetate + F- + CO2
-
decarboxylation is followed by release of F-
-
?
3-Fluoropyruvate
acetate + F- + CO2
-
decarboxylation is followed by release of F-
-
?
acetaldehyde + acetaldehyde
acetoin
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + acetaldehyde
acetoin
-
carboligation of 2 aldehydes as a side reaction of PDC
-
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
carboligation of 2 aldehydes as a side reaction of PDC, high carboligase activity, more active than PDC from Zymomonas mobilis
(R)-phenylacetylcarbinol
?
acetaldehyde + benzaldehyde
(R)-1-phenyl-1-hydroxy-propane-2-one
-
carboligation of 2 aldehydes as a side reaction of PDC, less active than PDC from Saccharomyces cerevisiae
(R)-phenylacetylcarbinol
?
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
-
-
-
-
ir
benzaldehyde + pyruvate + H+
(1R)-phenylacetylcarbinol + CO2
-
-
-
-
ir
cinnamaldehyde
(2S,3R)-5-phenylpent-4-ene-2,3-diol + CO2
-
-
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
enzyme catalyzes a carboligation as side reaction
-
?
phenylpyruvate + acetaldehyde
3-hydroxy-1-phenyl-butan-2-one + CO2
enzyme catalyzes a carboligation as side reaction
-
?
pyruvate
acetaldehyde + CO2
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
acetaldehyde + CO2
Acetobacter pasteurianus NCIB 8618 / ATCC 12874
key enzyme for the oxidative metabolism of lactic acid
-
?
pyruvate
acetaldehyde + CO2
ethanol fermentation pathway, involved in anaerobic metabolism
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, contains catalytic and regulatory pyruvate binding site
-
?
pyruvate
acetaldehyde + CO2
-
key enzyme at the branching point of alcoholic fermentation and respiration, expression at high glucose and low oxygen concentration
-
?
pyruvate
acetaldehyde + CO2
Pdc is involved in the operation of ethanolic fermentation pathway that appears to correlate to an extent with anoxia tolerance in plants, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80°C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor), 60% at pH 10.2 (80°C)
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
4 active sites in the tetramer, enzyme structure
-
?
pyruvate
acetaldehyde + CO2
-
alternating sites mechanism
-
?
pyruvate
acetaldehyde + CO2
-
catalytic cycle, 3 domains: a diphosphate-binding domain, a pyrimidine-binding domain and a regulatory domain, model for enzyme regulation
-
?
pyruvate
acetaldehyde + CO2
-
catalytic mechanism, acetaldehyde is produced by protonation of the key C2alpha-carbanion/enamine intermediate
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism with roles for the active center acid-base groups D28, E477, H114 and H115, catalytic cycle, mechanistic model of the reaction, alternating sites model
-
ir
pyruvate
acetaldehyde + CO2
-
detailed mechanism, catalytic cycle, alternating sites mechanism based on tight communication between active sites of the functional dimer, with the ionizable residues D28, E477 and H115 likely to be important in creating this communication, enzyme exists in three conformations, one inactive and two active forms, enzyme structure
-
ir
pyruvate
acetaldehyde + CO2
-
nonoxidative decarboxylation, main reaction
-
?
pyruvate
acetaldehyde + CO2
-
enzyme occupies the branch point between the oxidative metabolism of carbohydrates through the tricarboxylic acid cycle/electron-transport chain and the fermentative metabolism, hysteretically regulated by pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
enzyme within the glycolytic pathway in fermenting cells
-
?
pyruvate
acetaldehyde + CO2
-
key role in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step of alcohol fermentation
-
ir
pyruvate
acetaldehyde + CO2
-
regulation, glucose sensors Gpr1, Snf3 and Rgt2 are not involved, mutational analysis, overview
-
-
?
pyruvate
acetaldehyde + CO2
-
4 active sites in the tetramer, enzyme structure
-
?
pyruvate
acetaldehyde + CO2
-
penultimate step in the alcoholic fermentation process
-
?
pyruvate
acetaldehyde + CO2
-
only the undissociated pyruvic acid acts as the substrate
-
?
pyruvate
acetaldehyde + CO2
nonoxidative decarboxylation
-
?
pyruvate
acetaldehyde + CO2
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
nonoxidative decarboxylation
-
?
pyruvate
acetaldehyde + CO2
Sarcina ventriculi Goodsir / ATCC 55887
during growth in acidic environments, where acetate is toxic, expression of PDC serves to direct the flow of pyruvate into ethanol during fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
-
in wild-type, about 10% of the acetolactate forming activity
-
?
pyruvate
acetaldehyde + CO2
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
in wild-type, about 10% of the acetolactate forming activity
-
?
pyruvate
acetaldehyde + CO2
involved in the enhancement of ethanol production in berries, but not the limiting factor
-
?
pyruvate
acetaldehyde + CO2
enzyme expression is regulated by hypoxia and carbon source but posttranscriptional regulation may play a major role in regulating the metabolic flux
-
-
?
pyruvate
acetaldehyde + CO2
-
-
first enzyme in a branch of glycolysis that converts pyruvate to ethanol
?
pyruvate
acetaldehyde + CO2
key enzyme in alcoholic fermentation
-
?
pyruvate
acetaldehyde + CO2
key enzyme in alcoholic fermentation
-
?
pyruvate
acetaldehyde + CO2
-
-
-
-
?
pyruvate
acetaldehyde + CO2
-
active site structure, catalytic mechanism
-
?
pyruvate
acetaldehyde + CO2
C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation
-
?
pyruvate
acetaldehyde + CO2
-
H113 is involved in substrate binding and mediates the opening and closing of the active site by ion pairing with the carboxyl group of pyruvate
-
?
pyruvate
acetaldehyde + CO2
-
nonoxidative decarboxylation, main reaction
-
?
pyruvate
acetaldehyde + CO2
-
catalyzes the penultimate step in ethanol fermentation
-
?
pyruvate
ethanal + CO2
0.6% of the activity with 2-oxoisovalerate
-
-
?
pyruvate + acetaldehyde
acetoin + CO2
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor
i.e. 3-hydroxy-2-butanone, formation of the (R)- and the (S)-enantiomers
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
-
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
E477Q and D28A YPDC variants, via an enamine intermediate bound to the thiamine diphosphate cofactor, stereospecific reaction, overview
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
stereospecific reaction, optimization of the biotransformation assay method
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
carboligation reaction
-
-
?
pyruvate + benzaldehyde
(R)-phenylacetylcarbinol + CO2
-
wild-type 100% conversion, 98% enantiomeric excess, mutant I472A, 60% conversion, 70% enantiomeric excess, mutant I476E, 6% conversion, 60% enantiomeric excess of S-enantiomer
-
-
?
additional information
?
-
-
even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
involved in fruit ripening and aroma biogenesis
-
-
?
additional information
?
-
involved in fruit ripening and aroma biogenesis
-
-
?
additional information
?
-
-
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
?
additional information
?
-
involved in general metabolism to support energy production and biosynthesis of higher molecular weight compounds
-
-
?
additional information
?
-
no substrate: indole-3-pyruvate
-
-
?
additional information
?
-
no substrate: indole-3-pyruvate
-
-
?
additional information
?
-
-
no substrate: indole-3-pyruvate
-
-
?
additional information
?
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
no activity with benzoylformate, 3-hydroxyphenylpyruvate and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity with 3-phenyl-2-oxopropanoate, benzoyl formate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity with 3-phenyl-2-oxopropanoate, benzoyl formate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
isoform Pdc5p lacks enzymatic activity
-
-
?
additional information
?
-
-
isoform Pdc5p lacks enzymatic activity
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
substrate specificity of the engineered KdcA mutant enzymes with branched and unbranched 2-oxo acid substrates, overview
-
-
?
additional information
?
-
-
involved in aerobic fermentation in mature pollen
-
-
?
additional information
?
-
-
no activity is recorded on 3-phenyl-2-oxopropanoate, benzoylformate, 4-hydroxyphenylpyruvate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
no activity is recorded on 3-phenyl-2-oxopropanoate, benzoylformate, 4-hydroxyphenylpyruvate, and indole-3-pyruvate
-
-
?
additional information
?
-
-
critical enzyme in a pollen-specific pathway to bypass pyruvate dehydrogenase enzymes and maintain biosynthetic capacity and energy production under the unique conditions prevailing during pollen-pistil interaction
-
-
?
additional information
?
-
-
the enzyme catalyzes the penultimate step in alcohol fermentation
-
-
?
additional information
?
-
-
the role of the protein component of pyruvate decarboxylase in the mechanism of substrate activation
-
-
?
additional information
?
-
-
catalyzes also carboligase reactions in which the central enamine intermediate reacts with acetaldehyde or pyruvate, instead of the usual proton electrophile, resulting in the formation of acetoin and acetolactate, respectively, typically 1% of the total reaction, stereochemistry of products
-
?
additional information
?
-
-
enzyme catalyzes a carboligase reaction as side reaction forming acetoin and acetolactate
-
?
additional information
?
-
-
enzyme catalyzes also a carboligation as side reaction producing acetoin and acetolactate, mechanism, not: pyruvamide
-
?
additional information
?
-
-
oxidative diversion of the decarboxylation of pyruvate by 2,6-dichlorophenolindophenol, which traps a carbanionic intermediate and diverts the product from acetaldehyde to acetate, kinetics
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
in the pyruvamide-activated enzyme form, the flexible loop located on the beta-domain can transfer information to the active center thiamine diphosphate located at the interface of the alpha and gamma domains, overview
-
-
?
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
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
enzymatic stereoselective synthesis of L-norephedrine by coupling recombinant R-selective pyruvate decarboxylase from from Saccharomyces cerevisiae and an S-selective omega-transaminase from Vibrio fluvialis JS17, method optimization, overview
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
apart from the decarboxylation reaction, pyruvate decarboxylases are also known for their carboligation capabilities. During this reaction, the active aldehyde in the active site is condensed with a second aldehyde as a cosubstrate to form hydroxy ketones, when the co-substrate is acetaldehyde, (R)-acetoin is formed
-
-
?
additional information
?
-
-
the enzyme also performs carboligation reactions
-
-
?
additional information
?
-
-
one of the key enzymes involved in fermentation process
-
-
?
additional information
?
-
-
involved in a pathway in which NAD+ is regenerated under anaerobic conditions
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?
additional information
?
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nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
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?
additional information
?
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nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
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?
additional information
?
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nonoxidative decarboxylation of pyruvate and other 2-oxo-acids
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?
additional information
?
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even with benzaldehyde as the only substrate no benzoin can be detected, the enzyme does not produce (S)-2-hydroxypropiophenone
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?
additional information
?
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key enzyme in glycolytic pathway to ethanol
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?
additional information
?
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the enzyme catalyzes the penultimate step in alcohol fermentation
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?
additional information
?
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PDC has no activity with benzoylformate
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?
additional information
?
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pyruvate decarboxylase is one enzyme component of the pyruvate dehydrogenase complex
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?
