Information on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring)

New: Word Map on EC 1.2.4.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.2.4.1
-
RECOMMENDED NAME
GeneOntology No.
pyruvate dehydrogenase (acetyl-transferring)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetyl CoA biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Citrate cycle (TCA cycle)
-
-
Glycolysis / Gluconeogenesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
NIL
-
-
oxidative decarboxylation of pyruvate
-
-
pyruvate decarboxylation to acetyl CoA
-
-
Pyruvate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating)
Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-20-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ST
-
-
Manually annotated by BRENDA team
strain ST
-
-
Manually annotated by BRENDA team
microsporidia, uncertain whether pyruvate dehydrogenase is used in acetyl-CoA synthesis and whether the entire pyruvate dehydrogenase complex is present in microsporidia
-
-
Manually annotated by BRENDA team
E1alpha component of the pyruvate dehydrogenase multienzyme complex PDH
-
-
Manually annotated by BRENDA team
var. suum
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
sugar beet, cv. TK81-O, type 2 variant of the E1alpha subunit
-
-
Manually annotated by BRENDA team
analysis of enzyme phylogeny
SwissProt
Manually annotated by BRENDA team
fragment; strain 501R3
UniProt
Manually annotated by BRENDA team
fragment; strain 501R3
UniProt
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
subspecies Fundulus heteroclitus heteroclitus
-
-
Manually annotated by BRENDA team
Hansenula miso
-
-
-
Manually annotated by BRENDA team
Hansenula sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
organism contains only one single enzyme complex
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
regulatory role of pirin in the process of pyruvate catabolism through interaction with enzyme and inhibition of pyruvate dehydrogenase complex
-
-
Manually annotated by BRENDA team
cv. romano
Uniprot
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
expression in Lactococcus lactis
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
deletion of the E1a or E3 subunit genes of Plasmodium yoelii PDH causes no defect in blood stage development, mosquito stage development or early liver stage development. However, the gene deletions completely block the ability of the e1alpha- and e3-deficient parasites to form exo-erythrocytic merozoites during late liver stage development, thus preventing the initiation of a blood stage infection
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxyethylidene-thiamine diphosphate + 2,6-dichlorophenolindophenol
S-acetyldihydrolipoamide + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
2-keto-4-methylhexanoic acid + CoA + NAD+
3-methylpentanoyl-CoA + CO2 + NADH
show the reaction diagram
-
no substrate for wild-type, but for mutants I472A, I476F
-
-
?
2-ketobutanoate + CoA + NAD+
propanoyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-ketohexanoate + CoA + NAD+
pentanoyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
2-ketopentanoate + CoA + NAD+
butanoyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
alpha-ketobutyrate + Fe(CN)63- + H2O
hydroxyacetate + CO2 + Fe(CN)64-
show the reaction diagram
-
-
-
?
alpha-ketobutyrate + lipoamide
S-propionyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
?
benzoylformate + CoA + NAD+
benzoyl-CoA + CO2 + NADH
show the reaction diagram
-
no substrate for wild-type, but for mutants I472A, I476F
-
-
?
pyruvate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
pyruvate + acetylphosphinate + NAD+
(R)-acetoin + ? + NADH
show the reaction diagram
-
-
-
-
?
pyruvate + acetylphosphinate + NAD+
(S)-acetoin + ? + NADH
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + ?
show the reaction diagram
pyruvate + CoA + 2,6-dichlorophenolindophenol
acetyl-CoA + CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
show the reaction diagram
pyruvate + E2p lipoyl domain
acetylated E2p lipoyl domain + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + Fe(CN)63- + H2O
CO2 + Fe(CN)64-
show the reaction diagram
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
show the reaction diagram
pyruvate + pyruvate dehydrogenase complex subunit E2p
?
show the reaction diagram
-
-
-
-
?
pyruvate + [dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
show the reaction diagram
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
show the reaction diagram
pyruvate + [dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine
[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
-
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
additional information
-
CoA and NAD+ required by pyruvate dehydrogenase complex
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
-
can replace Mg2+
additional information
-
no activation by other divalent cations, except Mg2+, Mn2+, Ca2+, Ni2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
-
(3,4-dichlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
-
(3-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
-
(4-chlorophenyl)(dimethoxyphosphoryl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
-
(dimethoxyphosphoryl)(4-methylphenyl)methyl [3-(trifluoromethyl)phenoxy]acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (2,3-dichlorophenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (2,6-dichlorophenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (2-chloro-5-methylphenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (3-fluorophenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chloro-2-methylphenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chloro-3-methylphenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (4-chlorophenoxy)acetate
-
-
(dimethoxyphosphoryl)(phenyl)methyl (4-fluorophenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (2,3-dichlorophenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (2,6-dichlorophenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (2-chloro-5-methylphenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (3-fluorophenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (4-chloro-2-methylphenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (4-chloro-3-methylphenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (4-chlorophenoxy)acetate
-
-
1-(dimethoxyphosphoryl)ethyl (4-fluorophenoxy)acetate
-
-
2,2'-Dithiopyridine
-
1.1 mM, 30% inhibition
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (2,3-dichlorophenoxy)acetate
-
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (2-chloro-5-methylphenoxy)acetate
-
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (3-fluorophenoxy)acetate
-
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chloro-2-methylphenoxy)acetate
-
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chloro-3-methylphenoxy)acetate
-
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-chlorophenoxy)acetate
-
-
2,2,2-trichloro-1-(dimethoxyphosphoryl)ethyl (4-fluorophenoxy)acetate
-
-
2,3-Butanedione
Pigeon
-
10 mM, biphasic kinetic, complete inactivation after 20 min
2-p-Toluidinonaphthalene-6-sulfonate
-
-
3-Bromopyruvate
5,5'-dithiobis(2-nitrobenzoate)
acetaldehyde
-
weak
acetyl-CoA
acetylmethylphosphinate
Acetylphosphinate
AgNO3
-
18 mol per mol enzyme, complete inhibition
alpha-Ketobutyric acid
-
-
alpha-Ketocaproate
-
-
alpha-ketooctanoic acid
-
-
alpha-ketovalerate
-
-
Aluminium sulfate
-
1.1 mM, 35% inhibition
Ba2+
-
0.11 mM, 10% inhibition
beta-Hydroxypyruvate
Cd2+
-
0.032 mM, complete inhibition
citrate
Cu2+
-
0.36 mM, complete inhibition
D-glucose
-
treatment of cardiac fibroblasts with 35 mM D-glucose for 72 h reduces the PDH activity remarkably. 0.2 mM thiamine dramatically recovers the high glucose-induced PDH inhibition
diethyldicarbonate
Pigeon
-
-
EDTA
-
0.036 mM, 40% inhibition, 0.36 mM, complete inhibition, reversed by addition of excess Mg2+ and Ca2+
Fluoropyruvate
gibberellin
-
modulates the activity of enzyme by regulating the expression of pyruvate dehydrogenase kinase1 and subsequently controlling plant growth and development
glyoxylate
glyoxylic acid
-
weak
GTP
-
5 mM, about 50% inhibition after 3 h
illumination
-
mitochondrial pyruvate dehydrogenase complex
-
KCl
-
at 2 M, 50% residual activity of enzyme expressed in Escherichia coli
L-lactate
-
weak
methyl acetylphosphonate
-
phosphonate analogue of pyruvate, leading to formation of a stable 1,4-imino-2-alpha-phosphonolactyl-thiamindiphosphate
Methylacetylphosphonate
-
-
MgATP2-
Mn2+
-
0.72 mM
Moniliformin
-
0.3 mM, 82% inhibition
N-ethylmaleimide
-
1.1 mM, 50% inhibition
NaBH4
-
rapid inactivation in the presence of thiamine diphosphate, may reduce thiamine diphosphate to produce a reversible inhibitor
NaCl
-
at 2 M, 50% residual activity of enzyme expressed in Escherichia coli
O,O-dimethyl (2,3-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
-
O,O-dimethyl (2,3-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
-
O,O-dimethyl (2,4-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
-
O,O-dimethyl (2,4-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
-
O,O-dimethyl (2,6-dichlorophenoxyacetoxy)(furan-2-yl)-methylphosphonate
-
-
O,O-dimethyl (2,6-dichlorophenoxyacetoxy)(thien-2-yl)-methylphosphonate
-
-
O,O-dimethyl (2-chloro-5-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
O,O-dimethyl (2-chloro-5-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
-
O,O-dimethyl (3-fluorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
O,O-dimethyl (3-fluorophenoxyacetoxy)(thien-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-chloro-2-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-chloro-2-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-chloro-3-methylphenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-chloro-3-methylphenoxyacetoxy)(thien-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-chlorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-chlorophenoxyacetoxy)(thien-2-yl)methylphosphonate
-
-
O,O-dimethyl (4-fluorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
p-chloromercuribenzenesulfonate
-
8 mol per mol enzyme, complete inhibition
p-chloromercuribenzoate
PDC kinase II
-
phosphorylates and inactivates Pda1p
-
Phenylglyoxal
Pigeon
-
10 mM, biphasic kinetic, complete inactivation after 30 min
phenylpyruvate
-
-
Phosphorylation
protein Pkp1p
-
phosphorylates and inactivates Pda1p
-
Pyruvamide
-
acts as substrate analogue, competitive
pyruvate dehydrogenase kinase
Sodium diphosphate
-
competitive vs. thiamine diphosphate
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](2,4-dichlorophenyl)methyl]phosphonate
-
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](3-nitrophenyl)methyl]phosphonate
-
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](4-fluorophenyl)methyl]phosphonate
-
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](4-methoxyphenyl)methyl]phosphonate
-
-
sodium methyl [[[(2,4-dichlorophenoxy)acetyl]oxy](phenyl)methyl]phosphonate
-
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(2-chlorophenyl)methylphosphonate
-
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(3,4-dichlorophenyl)methyl phosphonate
-
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(4-chlorophenyl)methylphosphonate
-
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(4-methylphenyl)methylphosphonate
-
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(furan-2-yl)methylphosphonate
-
-
sodium o-methyl (2,4-dichlorophenoxyacetoxy)(pyridin-2-yl)methylphosphonate
-
-
tellurite
-
pyruvate dehydrogenase activity decreases by 81% after tellurite treatment (0.0005 mg/ml for 30 min)
-
Tetrahydrothiamine diphosphate
-
cis-isomer, 0.0013 mM, 50% inhibition
thiamine 2-thiazolone diphosphate
-
crystallization data of complex with enzyme
-
thiamine 2-thiothiazolone diphosphate
thiamine thiazolone diphosphate
thiamine thiothiazolone diphosphate
-
-
tryptamine-4,5-dione
-
inhibition is blocked by reduced glutathione or cysteine at large molar excess, ascorbate protects partially
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
stimulates
AMP
-
ascites tumour cells, 1 mM, about 2fold activation of pyruvate dehydrogenase
cAMP
-
ascites tumour cells
dobutamine
-
increases pyruvate dehydrogenase complex activity
fatty acid transport protein 1
-
enhances mitochondrial pyruvate dehydrogenase activity
-
GMP
-
ascites tumour cells
GTP
-
1-10 mM, slight activation
PDC phosphatase II
-
dephosphorylates and reactivates phosphorylated Pda1p
-
protein Ppp1p
-
dephosphorylates and reactivates phosphorylated Pda1p
-
pyruvate dehydrogenase kinase
-
dephosphorylation by pyruvatedehydrogenase phosphatase isoforms restores pyruvate dehydrogenase complex activity
-
pyruvate dehydrogenase phosphatase
spermine
-
in the absence of exogenous Ca2+ and Mg2+ and in the presence of EGTA, which favours the release of endogenous Ca2+, spermine is able to stimulate the activity of pyruvate dehydrogenase complex (maximum stimulation of about 140% at 0.5mM after 30 min of incubation, at concentrations higher than 0.5mM, spermine still stimulates PDC, when compared with the control, but shows a slight dose-dependent decrease). The interaction of spermine with PDC may also involve activation of pyruvate dehydrogenase kinase, resulting in an increase in E1alpha phosphorylation and consequently reduced stimulation of PDC at high polyamine concentrations
thiamine diphosphate
-
exogenous addition activates, involved in conformational changes
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7 - 40
2-keto-4-methylhexanoate
4.7 - 50
2-ketobutanoate
0.166
2-Ketobutyrate
-
-
0.2 - 12.7
2-ketohexanoate
2.5 - 7.6
2-ketopentanoate
1.8 - 4.4
benzoylformate
0.004 - 0.012
CoA
0.003
coenzyme A
-
assay with whole enzyme complex
0.73
E2p lipoyl domain
-
wild type enzyme, at pH 7.0 and 30C
-
0.02 - 0.027
lipoyl domain
0.36 - 1
Mg2+
15
N-acetyl-GDLLAEIETDK(lipoyl)-ATIG-amide
-
-
0.052
N-terminal lipoyl domain
-
-
-
0.033 - 0.07
NAD+
0.0002 - 50
pyruvate
0.00008 - 0.065
thiamine diphosphate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 8.1
2-keto-4-methylhexanoate
9 - 320
2-ketobutanoate
0.8 - 130
2-ketohexanoate
11 - 220
2-ketopentanoate
1.2 - 6.9
benzoylformate
0.08 - 95
E2p lipoyl domain
0.9 - 1.1
lipoyl domain
5
N-acetyl-GDLLAEIETDK(lipoylated)ATIG-amide
Mammalia
-
-
26.3 - 70
N-terminal lipoyl domain
0.077 - 486
pyruvate
0.35 - 1.39
thiamine diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
2-p-Toluidinonaphthalene-6-sulfonate
-
assay with whole enzyme complex, competitive inhibition
0.02
acetyl-CoA
-
competitive inhibition vs. CoA, whole enzyme complex
0.00146 - 0.0033
acetylmethylphosphinate
0.000014 - 0.00076
Acetylphosphinate
2.25
alpha-Ketobutyric acid
-
assay with whole enzyme complex
1
beta-Hydroxypyruvate
-
assay with whole enzyme complex
0.028
Bromopyruvate
-
assay with whole enzyme complex
8.6
citrate
-
-
0.0014 - 0.02
Fluoropyruvate
0.3 - 3.27
glyoxylate
0.5
glyoxylic acid
-
assay with whole enzyme complex
0.11
Hydroxypyruvate
-
-
0.015
NADH
-
competitive inhibition vs. NAD+, whole enzyme complex
0.02
Pyruvamide
-
pH 7.6, 30C, overall reaction of complex
31 - 37
pyruvate
0.51
Sodium diphosphate
-
-
0.000003
thiamine 2-thiazolone diphosphate
-
-
-
0.000064 - 0.0000737
thiamine 2-thiothiazolone diphosphate
0.003
thiamine thiazolone diphosphate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00085
-
enzyme from chloroplast
0.00265
-
enzyme from chloroplast
0.0048
-
Y177A mutant enzyme, 2,6-dichlorophenolindophenol assay, substrate 2alpha-hydroxyethyl-thiamin diphosphate
0.00485
-
enzyme from mitochondrion
0.00574
in cells grown on 50 mM glucose and 2 mM acetate, at 22C
0.00671
-
Y177F mutant enzyme, 2,6-dichlorophenolindophenol assay, substrate 2alpha-hydroxyethyl-thiamin diphosphate
0.0098
-
wild-type enzyme, 2,6-dichlorophenolindophenol assay, substrate 2alpha-hydroxyethyl-thiamin diphosphate
0.01
-
mutant I476F, substrate benzoylformate, 30C, pH 6.5
0.011
in cells grown on 50 mM glycerol and 2 mM acetate, at 22C
0.0162
-
recombinant His-tagged-alpha2,beta2 tetramer, assay with 2-hydroxyethylidene-thiamine diphosphate and 2,6-dichlorphenolindophenol
0.0269
-
recombinant His-tagged-alpha2,beta2 tetramer, assay with pyruvate and 2,6-dichlorphenolindophenol
0.035
-
pyruvate as substrate, pyruvate dehydrogenase preparation with high activity
0.0513
-
assay with whole enzyme complex
0.063
-
decarboxylation in the absence of K3Fe(CN)6 as artificial electron acceptor
0.085
-
pyruvate-K3Fe(CN)6 reductase assay
0.087
-
Y177A mutant enzyme, 2,6-dichlorophenolindophenol assay, substrate pyruvate
0.13
-
recombinant alpha2beta2 tetramer
0.14
-
pyruvate-K3Fe(CN)6 reductase assay
0.1416
-
decarboxylation in the presence of K3Fe(CN)6 as artificial electron acceptor
0.145
-
recombinant alpha2,His-tagged-beta2 tetramer, K3Fe(CN)6 as artificial electron acceptor
0.16
-
N-terminal lipoyl domain as substrate, pyruvate dehydrogenase preparation with high activity
0.18
-
recombinant alpha2,beta2 tetramer with six histidine residues attached to the N-terminus
0.187
-
recombinant His-tagged-alpha2,beta2 tetramer, K3Fe(CN)6 as artificial electron acceptor
0.216
-
Y177F mutant enzyme, 2,6-dichlorophenolindophenol assay, substrate pyruvate
0.367
-
recombinant alpha2,His-tagged-beta2 tetramer, assay with pyruvate and 2,6-dichlorphenolindophenol
0.385
-
purified recombinant wild-type E1, with 2,6-dichlorophenolindophenol as electron acceptor
0.445
-
wild-type enzyme, 2,6-dichlorophenolindophenol assay, substrate pyruvate
0.5
-
mutant I472A/I472A, substrate benzoylformate, 30C, pH 6.5
1.5
-
mutant I472A, substrate 2-keto-4-methylhexanoate, 30C, pH 6.5; mutant I472A, substrate benzoylformate, 30C, pH 6.5
2
-
mutant I472A/I472A, substrate pyruvate, 30C, pH 6.5
2.2
-
mutant I472A/I472A, substrate 2-ketobutanoate, 30C, pH 6.5
2.5
-
mutant I472A/I472A, substrate 2-keto-4-methylhexanoate, 30C, pH 6.5
2.7
-
mutant I476F, substrate 2-ketopentanoate, 30C, pH 6.5
3.26
-
recombinant enzyme from testis
5.7
-
assay with whole enzyme complex
7.3
-
mutant I472A/I472A, substrate 2-ketopentanoate, 30C, pH 6.5
8
-
mutant I476F, substrate 2-ketobutanoate, 30C, pH 6.5
8.13
-
recombinant enzyme from liver
10.9
-
recombinant alpha2,His-tagged-beta2 tetramer, reduction of NAD+, overall reaction
13
-
wild-type, substrate 2-ketopentanoate, 30C, pH 6.5
14.4
-
recombinant His-tagged-alpha2,beta2 tetramer, reduction of NAD+, overall reaction
15.8
-
reduction of NAD+, overall reaction
19
-
mutant I476F, substrate pyruvate, 30C, pH 6.5
20
-
mutant I472A/I472A, substrate 2-ketohexanoate, 30C, pH 6.5
24.6
-
pH 7.0, 37C, isoform PDH2
25.9
-
pH 7.0, 37C, isoform PDH1
28.35
-
purified recombinant wild-type E1, with NAD+ as electron acceptor
32
-
mutant I472A, substrate 2-ketohexanoate, 30C, pH 6.5
50
-
mutant I472A, substrate pyruvate, 30C, pH 6.5
54
-
mutant I472A, substrate 2-ketopentanoate, 30C, pH 6.5
55
-
recombinant enzyme from Haloferax volcanii
62
-
mutant I472A, substrate 2-ketobutanoate, 30C, pH 6.5
79
-
wild-type, substrate 2-ketobutanoate, 30C, pH 6.5
91
-
recombinant enzyme from Escherichia coli
120
-
wild-type, substrate pyruvate, 30C, pH 6.5
1791
-
activity after reassociation of the purified enzyme with EC 2.3.1.12 and EC 1.8.1.4
additional information
-
measurement of NADH/NAD+ and acetyl-CoA/CoA ratios, and citric acid cycle intermediates in blood and tissue, measurement of O2-uptake and fatty acid and glucose oxidation level
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
-
6.5 - 7
-
with Mg2+ as divalent cation
6.5 - 7.5
-
with Ca2+ as divalent cation
7.4
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
wild-type enzyme
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
-
value for pyruvate dehydrogenase complex
additional information
-
temperature dependence of wild-type and mutant enzymes
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
non-small cell lung carcinoma
Manually annotated by BRENDA team
-
type 2 variant of the E1alpha subunit, most abundant expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
absent in the mitochondrion
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O157:H7 (strain TW14359 / EHEC)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
SDS-PAGE
99470
pyruvate dehydrogenase multienzyme complex component E1
100000
-
sucrose density gradient centrifugation
136000
-
gel filtration
150000
-
calculation from sedimentation and diffusion data, low speed sedimentation equilibrium centrifugation, meniscus depletion method
160000
-
recombinant alpha2,beta2 tetramer
169000
-
whole pyruvate dehydrogenase enzyme complex, gel filtration
182000 - 183000
190000
-
sedimentation equilibrium centrifugation
200000
-
SDS-PAGE
206000
-
scanning transmission electron microscopy
240000
-
gel filtration, recombinant protein from Escherichia coli and from Haloferax volcanii
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY