Information on EC 1.2.1.51 - pyruvate dehydrogenase (NADP+)

for references in articles please use BRENDA:EC1.2.1.51
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.2.1.51
-
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RECOMMENDED NAME
GeneOntology No.
pyruvate dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyruvate + CoA + NADP+ = acetyl-CoA + CO2 + NADPH
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetyl-CoA biosynthesis II (NADP-dependent pyruvate dehydrogenase)
-
-
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 methylviologen as acceptor, more slowly. The enzyme is inhibited by oxygen.
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CAS REGISTRY NUMBER
COMMENTARY hide
93389-35-6
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and strain 124A
-
-
Manually annotated by BRENDA team
and strain 124A
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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
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
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
thiamine diphosphate
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
-
-
2',5'-ATP-ribose
-
-
CO2
-
product inhibition
Quinacrine
-
-
additional information
-
not arsenite
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
-
dependent on
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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
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.93
-
3-hydroxypyruvate
2.36
-
2-oxobutyrate
2.6
-
oxaloacetate
14.3
-
pyruvate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
confirmed by immuno fluorescence microscopy
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
166000
-
2 * 166000, SDS-PAGE
190000
-
2 * 190000, SDS-PAGE
195000
2 * 195000, calculation from sequence
217000
-
calculated from cDNA
309000
320000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.51)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)