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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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EC Tree
IUBMB Comments The Euglena enzyme can also use FAD or methylviologen as acceptor, more slowly. The enzyme is inhibited by oxygen.
The enzyme appears in viruses and cellular organisms
Synonyms
pyruvate dehydrogenase, pyruvate:nadp+ oxidoreductase, cppno,
more
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pyruvate dehydrogenase
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-
pyruvate:NADP+ oxidoreductase
PDH
-
-
pyruvate:NADP+ oxidoreductase
-
-
pyruvate:NADP+ oxidoreductase
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-
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pyruvate + CoA + NADP+ = acetyl-CoA + CO2 + NADPH
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-
-
-
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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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2-oxobutyrate + CoA + NADP+
propionyl-CoA + CO2 + NADPH
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-
-
-
?
3-hydroxypyruvate + CoA + NADP+
hydoxyacetyl-CoA + CO2 + NADPH
-
-
-
-
?
oxaloacetate + CoA + NADP+
? + CO2 + NADPH
-
-
-
-
?
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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-
-
-
?
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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-
-
-
r
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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-
-
r
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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NADP+ can be substituted by methyl viologen
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-
r
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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NADP+ can be substituted by benzyl viologen
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-
r
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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reverse reaction 2% of forward reaction
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-
r
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pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
-
-
-
-
?
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
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-
-
-
r
pyruvate + CoA + NADP+
acetyl-CoA + CO2 + NADPH
Q94IN5
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-
-
r
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NADP+
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not NAD+
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Fe
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4 mol per mol subunit
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additional information
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not arsenite
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thiamine diphosphate
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dependent on
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0.068
methyl viologen
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-
additional information
additional information
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kinetic mechanism
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0.0066
CoA
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with NADP+
0.0081
CoA
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with methyl viologen
0.028
NADP+
-
-
0.027
pyruvate
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with NADP+
0.033
pyruvate
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with methyl viologen
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brenda
and strain 124A
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-
brenda
and strain 124A
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-
brenda
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-
-
brenda
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Uniprot
brenda
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confirmed by immuno fluorescence microscopy
brenda
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-
brenda
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physiological function
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part of citric acid cycle
physiological function
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part of citric acid cycle
-
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PNO_CRYPV
1934
0
217557
Swiss-Prot
PNO_EUGGR
1803
0
199821
Swiss-Prot
B6KHE3_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
1027
0
113024
TrEMBL
A0A2G8YB35_TOXGO
277
0
29451
TrEMBL
B6AEJ2_CRYMR
Cryptosporidium muris (strain RN66)
1945
0
220349
TrEMBL
A0A086LC35_TOXGO
242
0
25365
TrEMBL
A0A139YAZ1_TOXGO
242
0
25333
TrEMBL
A0A086QHE1_TOXGO
1027
0
112964
TrEMBL
A0A086KWG5_TOXGO
1027
0
112948
TrEMBL
M9PA66_MASBA
1723
0
188123
TrEMBL
A0A0A1TYU8_ENTIV
1161
0
127872
TrEMBL
S7V0F8_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
1027
0
112948
TrEMBL
A0A0A1UF84_ENTIV
1161
0
127331
TrEMBL
A0A125YFL0_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
1027
0
113024
TrEMBL
A0A086M5Z5_TOXGO
784
0
87575
TrEMBL
A0A086QDP4_TOXGO
1027
0
113080
TrEMBL
A0A174Q0Z1_9BACE
157
0
18071
TrEMBL
G4E6K8_9GAMM
1646
0
181949
TrEMBL
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166000
-
2 * 166000, SDS-PAGE
190000
-
2 * 190000, SDS-PAGE
195000
2 * 195000, calculation from sequence
217000
-
calculated from cDNA
309000
-
gel filtration; II. NADPH-diaphorase fragment with associated FAD; I. methyl viologen-pyruvate dehydrogenase fragment with iron-sulfur cluster; two covalently linked domains
309000
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gel filtration; I. methyl viologen-pyruvate dehydrogenase fragment with iron-sulfur cluster; two covalently linked domains
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dimer
-
2 * 166000, SDS-PAGE
dimer
2 * 195000, calculation from sequence
dimer
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2 * 190000, SDS-PAGE
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the enzyme is stabilized by its cofactor, thiamine diphosphate, in mitochondria of Euglena gracilis
-
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O2 leads to rapid inactivation
-
288278, 288279, 288281, 288283
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Inui, H.; Yamaji, R.; Saidoh, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Pyruvate:NADP+ oxidoreductase from Euglena gracilis: limited proteolysis of the enzyme with trypsin
Arch. Biochem. Biophys.
286
270-276
1991
Euglena gracilis
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Pyruvate: NADP+ oxidoreductase from Euglena gracilis: mechanism of O2-inactivation of the enzyme and its stability in the aerobe
Arch. Biochem. Biophys.
280
292-298
1990
Euglena gracilis
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Pyruvate: NADP+ oxidoreductase from Euglena gracilis: the kinetic properties of the enzyme
Arch. Biochem. Biophys.
274
434-442
1989
Euglena gracilis
brenda
Inui, H.; Ono, K.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Purification and characterization of pyruvate:NADP+ oxidoreductase in Euglena gracilis
J. Biol. Chem.
262
9130-9135
1987
Euglena gracilis
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
The physiological role of oxygen-sensitive pyruvate dehydrogenase in mitochondrial fatty acid synthesis in Euglena gracilis
Arch. Biochem. Biophys.
237
423-429
1985
Euglena gracilis
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Occurrence of oxygen-sensitive, NADP+-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis
J. Biochem.
96
931-934
1984
Euglena gracilis
brenda
Nakazawa, M.; Inui, H.; Yamaji, R.; Yamamoto, T.; Takenaka, S.; Ueda, M.; Nakano, Y.; Miyatake, K.
The origin of pyruvate: NADP oxidoreductase in mitochondria of Euglena gracilis
FEBS Lett.
479
155-156
2000
Euglena gracilis (Q94IN5)
brenda
Lochmeyer, C.; Fuchs, G.
NADP+-specific 2-oxoglutarate dehydrogenase in denitrifying Pseudomonas species
Arch. Microbiol.
153
226-229
1990
Euglena gracilis
-
brenda
Nakazawa, M.; Takenaka, S.; Ueda, M.; Inui, H.; Nakano, Y.; Miyatake, K.
Pyruvate:NADP+ oxidoreductase is stabilized by its cofactor, thiamin pyrophosphate, in mitochondria of Euglena gracilis
Arch. Biochem. Biophys.
411
183-188
2003
Euglena gracilis
brenda
Ctrnacta, V.; Ault, J.G.; Stejskal, F.; Keithly, J.S.
Localization of pyruvate:NADP+ oxidoreductase in sporozoites of Cryptosporidium parvum
J. Eukaryot. Microbiol.
53
225-231
2006
Cryptosporidium parvum
brenda
Sawada, K.; Taki, A.; Yamakawa, T.; Seki, M.
Key role for transketolase activity in erythritol production by Trichosporonoides megachiliensis SN-G42
J. Biosci. Bioeng.
108
385-390
2009
Moniliella megachiliensis, Moniliella megachiliensis SN-G42
brenda
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