Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring) and Organism(s) Sus scrofa

for references in articles please use BRENDA:EC1.2.4.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex, EC 1.2.1.104, 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Sus scrofa
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
pdh, pdha1, mitochondrial pyruvate dehydrogenase, e1alpha, pyruvate dehydrogenase multienzyme complex, pyruvate dehydrogenase e1, pdhc-e1, mtpdc, pdhc e1, pyruvate dehydrogenase e1 component, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, pyruvate
-
-
-
-
MtPDC
-
-
-
-
pyruvate decarboxylase
-
-
-
-
pyruvate dehydrogenase
-
-
-
-
pyruvate dehydrogenase complex
-
-
-
-
pyruvic acid dehydrogenase
-
-
-
-
pyruvic dehydrogenase
-
-
-
-
VEG220
-
-
-
-
Vegetative protein 220
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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, EC 1.2.1.104, 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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + benzaldehyde
(R)-phenylacetylcarbinol
show the reaction diagram
-
-
-
-
?
alpha-ketobutyrate + lipoamide
S-propionyldihydrolipoamide + CO2
show the reaction diagram
-
-
-
?
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyruvate + lipoamide
S-acetyldihydrolipoamide + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
required
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-Dithiopyridine
-
1.1 mM, 30% inhibition
3-deazathiamine diphosphate
-
competitive inhibitor
5,5'-dithiobis(2-nitrobenzoate)
-
1.1 mM, 35% inhibition
AgNO3
-
18 mol per mol enzyme, complete inhibition
Aluminium sulfate
-
1.1 mM, 35% inhibition
Ba2+
-
0.11 mM, 10% inhibition
Cd2+
-
0.032 mM, complete inhibition
citrate
-
noncompetitive inhibition
Cu2+
-
0.36 mM, complete inhibition
EDTA
-
0.036 mM, 40% inhibition, 0.36 mM, complete inhibition, reversed by addition of excess Mg2+ and Ca2+
MgATP2-
-
due to phosphorylation of the enzyme by pyruvate dehydrogenase kinase
Mn2+
-
0.72 mM
N-ethylmaleimide
-
1.1 mM, 50% inhibition
Oxythiamine diphosphate
-
competitive inhibitor
p-chloromercuribenzenesulfonate
-
8 mol per mol enzyme, complete inhibition
p-chloromercuribenzoate
-
8 mol per mol enzyme, complete inhibition
phosphorylation
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
pyruvate
-
in the presence of Ca2+ and Mg2+
0.065
thiamine diphosphate
-
in the presence of Ca2+ and Mg2+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.6
citrate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000026
3-deazathiamine diphosphate
Sus scrofa
-
pH 7.8, temperature not specified in the publication
0.000025
Oxythiamine diphosphate
Sus scrofa
-
pH 7.8, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
-
with Mg2+ as divalent cation
6.5 - 7.5
-
with Ca2+ as divalent cation
9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ODPA_PIG
389
0
43121
Swiss-Prot
Mitochondrion (Reliability: 2)
A0A8D0IE49_PIG
361
0
39576
TrEMBL
Mitochondrion (Reliability: 2)
A0A5G2QSU5_PIG
361
0
39629
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D1WYA6_PIG
389
0
43294
TrEMBL
Mitochondrion (Reliability: 1)
Q9TRT3_PIG
15
0
1789
TrEMBL
other Location (Reliability: 1)
A0A8D0IBN5_PIG
360
0
39219
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D0X6F8_PIG
396
0
44017
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D0LRP0_PIG
414
1
46033
TrEMBL
other Location (Reliability: 4)
A0A5G2R718_PIG
341
0
37128
TrEMBL
other Location (Reliability: 3)
A0A8D1B2N4_PIG
363
0
39576
TrEMBL
Mitochondrion (Reliability: 2)
A0A4X1VDD8_PIG
341
0
37128
TrEMBL
other Location (Reliability: 3)
A0A8D2A4F3_PIG
372
0
41471
TrEMBL
other Location (Reliability: 4)
A0A4X1VIG0_PIG
360
0
39272
TrEMBL
Mitochondrion (Reliability: 2)
Q9TRT4_PIG
15
0
1757
TrEMBL
other Location (Reliability: 1)
A0A4X1VHD7_PIG
361
0
39629
TrEMBL
Mitochondrion (Reliability: 2)
A0A5K1VBH1_PIG
396
0
44017
TrEMBL
Mitochondrion (Reliability: 1)
A0A4X1V1M9_PIG
370
0
41173
TrEMBL
Mitochondrion (Reliability: 5)
Q9TRT5_PIG
15
0
1747
TrEMBL
other Location (Reliability: 1)
F1SGH5_PIG
360
0
39272
TrEMBL
Mitochondrion (Reliability: 2)
A0A4X1V4S1_PIG
390
0
43365
TrEMBL
Mitochondrion (Reliability: 2)
I3LCI2_PIG
376
0
41686
TrEMBL
Mitochondrion (Reliability: 2)
Q9GKJ2_PIG
35
0
3821
TrEMBL
other Location (Reliability: 2)
A0A8D1R8B1_PIG
376
0
41686
TrEMBL
Mitochondrion (Reliability: 2)
A0A480VQH5_PIG
390
0
43365
TrEMBL
Mitochondrion (Reliability: 2)
Q9TRT6_PIG
15
0
1787
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
136000
-
gel filtration
150000
-
calculation from sedimentation and diffusion data, low speed sedimentation equilibrium centrifugation, meniscus depletion method
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
inactivated by phosphorylation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51
-
1 min, complete inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 50 mM potassium phosphate, pH 7.0, 0.5 mM EDTA, several months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pyruvate dehydrogenase
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of pyruvate dehydrogenase complex
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kerbey, A.L.; Randle, P.J.
Pyruvate dehydrogenase kinase activity of pig heart pyruvate dehydrogenase (E1 component of pyruvate dehydrogenase complex)
Biochem. J.
231
523-529
1985
Sus scrofa
Manually annotated by BRENDA team
Hamada, M.; Hiraoka, T.; Koike, K.; Ogasahara, K.; Kanzaki, T.; Koike, M.
Properties and subunit structure of pig heart pyruvate dehydrogenase
J. Biochem.
79
1273-1285
1976
Sus scrofa
Manually annotated by BRENDA team
Eram, M.S.; Oduaran, E.; Ma, K..
The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis
Archaea
2014
349379
2014
Sus scrofa
Manually annotated by BRENDA team
Grabowska, E.; Czerniecka, M.; Czyzewska, U.; Zambrzycka, A.; Lotowski, Z.; Tylicki, A.
Differences in the efficiency of 3-deazathiamine and oxythiamine pyrophosphates as inhibitors of pyruvate dehydrogenase complex and growth of HeLa cells in vitro
J. Enzyme Inhib. Med. Chem.
36
122-129
2021
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team