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Information on EC 1.2.4.1 - pyruvate dehydrogenase (acetyl-transferring) and Organism(s) Rattus norvegicus
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1.2.4.1 pyruvate dehydrogenase (acetyl-transferring)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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Word Map
- 1.2.4.1
- acetyl-coa
- dichloroacetate
- cardiac
-
tricarboxylic
-
lipoylation
- glycogen
- tca
-
pituitary-dependent
- acidosis
- hyperadrenocorticism
- dihydrolipoamide
-
x-linked
- lipoamide
-
warburg
- stearothermophilus
-
lipoic
- acth
- cortisol
- lipoate
-
hyperpolarized
-
crustacean
- histoplasmosis
- leigh
-
pigment-dispersing
-
vastus
- hypercortisolism
-
ketogenic
- phosphocreatine
- transacetylase
-
maple
- histoplasma
- trilostane
- pyranose
-
anaplerosis
- capsulatum
-
hernia
-
alpha2beta2
- prephenate
- acetylcarnitine
-
antimitochondrial
-
interbody
- agriculture
- medicine
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pdh, pdha1, mitochondrial pyruvate dehydrogenase, e1alpha, pyruvate dehydrogenase multienzyme complex, pyruvate dehydrogenase e1, pdhc-e1, mtpdc, pdhc e1, pyruvate dehydrogenase e1 component, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, pyruvate
-
-
-
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MtPDC
-
-
-
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PDH
pyruvate decarboxylase
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-
-
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pyruvate dehydrogenase
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-
-
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pyruvate dehydrogenase complex
pyruvic acid dehydrogenase
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-
-
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pyruvic dehydrogenase
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-
-
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VEG220
-
-
-
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Vegetative protein 220
-
-
-
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PDH
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-
-
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pyruvate dehydrogenase complex
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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
9014-20-4
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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
additional information
?
-
-
determination of free short-chain CoA esters in rat heart
-
-
?
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
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enzyme is the E1alpha component of the pyruvate dehydrogenase multienzyme complex, regulation via reversible phosphorylation, age-related in crease in enzyme E1alpha activity due to age-related decline in pyruvate dehydrogenase kinase PDK-4, overview
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-
?
NATURAL SUBSTRATE
NATURAL 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
pyruvate + CoA + NAD+
acetyl-CoA + CO2 + NADH
-
enzyme is the E1alpha component of the pyruvate dehydrogenase multienzyme complex, regulation via reversible phosphorylation, age-related in crease in enzyme E1alpha activity due to age-related decline in pyruvate dehydrogenase kinase PDK-4, overview
-
-
?
additional information
?
-
-
determination of free short-chain CoA esters in rat heart
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
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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
additional information
-
there is no significant change in the PDH activity in the presence of D-mannitol (35 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
with aging of rats the Vmax of the enzyme complex increases by 60%, while the Km decreases by 1.6fold in the same time, enzyme expression level remaines constant, more efficient catabolization of pyruvate due to adaptive phosphorylation of the enzyme within the multienzyme complex, age-related decline in pyruvate dehydrogenase kinase PDK-4
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODPB_RAT
359
0
38982
Swiss-Prot
Mitochondrion (Reliability: 1)
ODPAT_RAT
391
0
43393
Swiss-Prot
Mitochondrion (Reliability: 5)
ODPA_RAT
390
0
43227
Swiss-Prot
Mitochondrion (Reliability: 1)
D4A5G8_RAT
381
0
42439
TrEMBL
Mitochondrion (Reliability: 2)
A0A0G2KAM3_RAT
411
0
45115
TrEMBL
other Location (Reliability: 1)
Q4FZZ4_RAT
390
0
43216
TrEMBL
Mitochondrion (Reliability: 1)
F7FKI5_RAT
378
0
41931
TrEMBL
Mitochondrion (Reliability: 1)
A0A8I6GKV6_RAT
390
0
43291
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8I6A8K3_RAT
423
0
46193
TrEMBL
other Location (Reliability: 1)
A0A0G2JW90_RAT
376
0
41787
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40315
-
x * 40315, pyruvate dehydrogenase multienzyme complex component E1alpha, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 40315, pyruvate dehydrogenase multienzyme complex component E1alpha, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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the O-glycosylation of PDH E1alpha is involved in the regulation of the PDH activity
phosphoprotein
phosphoprotein
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the enzyme, as pyruvate dehydrogenase multienzyme complex component E1alpha, becomes reversibly phosphorylated at 3 serine residues by specific pyruvate dehydrogenase kinases PDK1-4, and dephosphorylated by a specific pyruvate dehydrogenase phosphatase PDP-1 and to a lesser extant PDP-2, regulatory function, pyruvate oxidation is inhibited in phosphorylated state of E1alpha
phosphoprotein
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phosphorylation of the PDH E1alpha subunit by PDH kinase contributes to the suppression of PDH activity. Streptozotocin treatment causes a significant increase in the level of the phosphorylated PDH E1alpha subunit in the diabetic rat hearts
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of alpha subunit with human liver beta subunit in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high glucose loads do not alter the level of PDH mRNA expressions in cardiac fibroblasts
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the activity of pyruvate dehydrogenase is reduced in diabetic rats. Thiamine ameliorates diabetes-induced PDH inhibition by suppressing the increased expression of the O-glycosylated protein
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the O-glycosylated PDH protein is markedly increased in cardiac fibroblasts exposed to high glucose
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jeng, J.; Kallarakal, A.T.; Kim, S.F.; Popov, K.M.; Song, B.J.
Pyruvate dehydrogenase E1alpha isoform in rat testis: cDNA cloning, characterization, and biochemical comparison of the recombinant testis and liver enzymes
Comp. Biochem. Physiol. B
120
205-216
1998
Homo sapiens, Rattus norvegicus
Moreau, R.; Heath, S.H.D.; Doneanu, C.E.; Harris, R.A.; Hagen, T.M.
Age-related compensatory activation of pyruvate dehydrogenase complex in rat heart
Biochem. Biophys. Res. Commun.
325
48-58
2004
Rattus norvegicus
Kohda, Y.; Umeki, M.; Kono, T.; Terasaki, F.; Matsumura, H.; Tanaka, T.
Thiamine ameliorates diabetes-induced inhibition of pyruvate dehydrogenase (PDH) in rat heart mitochondria: investigating the discrepancy between PDH activity and PDH E1alpha phosphorylation in cardiac fibroblasts exposed to high glucose
J. Pharmacol. Sci.
113
343-352
2010
Rattus norvegicus
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Release 2023.1 (January 2023)
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