Information on EC 1.2.1.51 - pyruvate dehydrogenase (NADP+)

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

EC NUMBER
COMMENTARY hide
1.2.1.51
-
RECOMMENDED NAME
GeneOntology No.
pyruvate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyruvate + CoA + NADP+ = acetyl-CoA + CO2 + NADPH
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 II (NADP-dependent pyruvate dehydrogenase)
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-
oxidative decarboxylation of pyruvate
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-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:NADP+ 2-oxidoreductase (CoA-acetylating)
The Euglena enzyme can also use FAD or methyl viologen as acceptor, more slowly. The enzyme is inhibited by oxygen.
CAS REGISTRY NUMBER
COMMENTARY hide
93389-35-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SN-G42 and 124A
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-
Manually annotated by BRENDA team
strain SN-G42 and 124A
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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-oxobutyrate + CoA + NADP+
propionyl-CoA + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
3-hydroxypyruvate + CoA + NADP+
hydoxyacetyl-CoA + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
oxaloacetate + CoA + NADP+
? + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
show the reaction diagram
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 + NADP+
acetyl-CoA + CO2 + NADPH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
thiamine diphosphate
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
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-
2',5'-ATP-ribose
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-
CO2
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product inhibition
Quinacrine
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-
additional information
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not arsenite
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
dependent on
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0066 - 0.0081
CoA
0.068
methyl viologen
-
-
0.028 - 0.03
NADP+
0.027 - 0.21
pyruvate
additional information
additional information
-
kinetic mechanism
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.93
-
3-hydroxypyruvate
2.36
-
2-oxobutyrate
2.6
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oxaloacetate
14.3
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pyruvate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
confirmed by immuno fluorescence microscopy
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
217000
-
calculated from cDNA
309000
320000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stabilized by its cofactor, thiamine diphosphate, in mitochondria of Euglena gracilis
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
O2 leads to rapid inactivation
-
288278, 288279, 288281, 288283
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE