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Information on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring) and Organism(s) Bos taurus

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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.
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Bos taurus
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The taxonomic range for the selected organisms is: Bos taurus
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
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MtPDC
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PDH
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pyruvate decarboxylase
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pyruvate dehydrogenase
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pyruvate dehydrogenase complex
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pyruvic acid dehydrogenase
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pyruvic dehydrogenase
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VEG220
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Vegetative protein 220
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
show the reaction diagram
two-step reaction: thiamine diphosphate dependent decarboxylation of pyruvate to 2-hydroxyethylidene-thiamine diphosphate and subsequent reductive acetylation of lipoic acid residues bound to the dihydrolipoamide acetyltransferase, EC 2.3.1.12
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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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
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SUBSTRATE
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
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specific for
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?
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
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specific for
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphorylation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
pyruvate
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similar values
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.063
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decarboxylation in the absence of K3Fe(CN)6 as artificial electron acceptor
0.1416
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decarboxylation in the presence of K3Fe(CN)6 as artificial electron acceptor
15.8
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reduction of NAD+, overall reaction
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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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_BOVIN
390
0
43388
Swiss-Prot
Mitochondrion (Reliability: 1)
ODPB_BOVIN
359
0
39126
Swiss-Prot
Mitochondrion (Reliability: 2)
A0A3Q1MTX8_BOVIN
384
0
42303
TrEMBL
Mitochondrion (Reliability: 2)
A0A452DJH4_BOVIN
387
0
42972
TrEMBL
Mitochondrion (Reliability: 1)
Q2T9Y3_BOVIN
391
0
43292
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1MI08_BOVIN
386
0
42974
TrEMBL
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
154000
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36000
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alpha2,beta2, 2 * 41000 + 2 * 36000
41000
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alpha2,beta2, 2 * 41000 + 2 * 36000
additional information
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MW of native complex isolated from kidney and heart: 7000000 Da and 8500000 Da respectively
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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alpha2,beta2, 2 * 41000 + 2 * 36000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very sensitive to freezing and thawing
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very sensitive to proteolysis, especially during purification
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-50°C, 50 mM potassium phosphate buffer, pH 7.0, 1 mM MgCl2, 20 mM thiamine diphosphate, 0.1 mM EDTA, 0.4 mM DTT, 0.1 mM NAD+, several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pettit, F.H.; Reed, L.J.
Pyruvate dehydrogenase complex from bovine kidney and heart
Methods Enzymol.
89
376-386
1982
Bos taurus
Manually annotated by BRENDA team
Korotchkina, L.G.; Tucker, M.M.; Thekkumkara, T.J.; Madhusudhan, K.T.; Pons, G.; Kim, H.; Patel, M.S.
Overexpression and characterization of human tetrameric pyruvate dehydrogenase and its individual subunits
Protein Expr. Purif.
6
79-90
1995
Bos taurus, Homo sapiens
Manually annotated by BRENDA team