1.8.1.4: dihydrolipoyl dehydrogenase This is an abbreviated version! For detailed information about dihydrolipoyl dehydrogenase, go to the full flat file .
Reaction
protein N6-(dihydrolipoyl)lysine +
NAD+ =
protein N6-(lipoyl)lysine +
NADH +
H+
Synonyms apicoplast E3, CDS, CIP50, coronin-interacting protein, dehydrogenase, lipoamide, dehydrolipoate dehydrogenase, DHLDH, DHLipDH, diaphorase, dihydrolipoamide dehydrogenase, dihydrolipoamide dehydrogenase E3, dihydrolipoamide:NAD+ oxidoreductase, dihydrolipoic dehydrogenase, dihydrolipomide dehydrogenase, dihydrolipoyl dehydrogenase, DLD, DLD1, Dld2, DLDH, DLDH dehydrogenase, DLDH diaphorase, DLDH2, DT-diaphorase, E3, E3 component, E3 component of 2-oxoglutarate dehydrogenase complex, E3 component of acetoin cleaving system, E3 component of alpha keto acid dehydrogenase complexes, E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes, E3 component of pyruvate complex, E3 lipoamide dehydrogenase, E3 protein component of 2-oxoacid dehydrogenase multienzyme complexes, E3 subunit of the alpha-ketoglutarate dehydrogenase complex, EC 1.6.4.3, Glycine cleavage system L protein, Glycine oxidation system L-factor, hDLDH, hE3, hLADH, L-protein, LAD, LADH, LDH, LDP-Glc, LDP-Val, LipDH, lipoamide dehydrogenase, lipoamide dehydrogenase (NADH), lipoamide dehydrogenase C, lipoamide dehydrogenase2, lipoamide oxidoreductase (NADH), lipoamide reductase, lipoamide-dehydrogenase-valine, lipoate dehydrogenase, lipoic acid dehydrogenase, lipoyl dehydrogenase, LPD, LPD-GLC, LPD-VAL, LPD1, LPD2, Lpd3, LpdA, LpdC, LpdG, LpdV, More, mtLPD2, NAD(P)H:lipoamide oxidoreductase, NADH dehydrogenase, NADH diaphorase, NADH:lipoamide oxidoreductase, nicotinamide adenine dinucleotide diaphorase, ORF-E3, pdhD, pdhL, PfaE3, rhDLDH, TAase, ubiquinone reductase
ECTree
Cofactor
Cofactor on EC 1.8.1.4 - dihydrolipoyl dehydrogenase
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dihydrolipoic acid
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-
FAD
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-
FAD
Starkeyomyces koorchalomoides
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-
FAD
-
contains 1 FAD per subunit
FAD
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contains 1 FAD per subunit
FAD
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contains 1 FAD per subunit
FAD
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contains 1 FAD per subunit
FAD
-
contains 1 FAD per subunit
FAD
-
contains 1 FAD per subunit
FAD
-
contains 1 FAD per subunit
FAD
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contains 1 FAD per subunit
FAD
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wild-type enzyme contains 1 FAD per subunit, mutant enzymes K54E and S53K/K54S have about 25% less bound FAD
FAD
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0.01882 mM of FAD per mg of protein
FAD
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2 molecules of FAD per molecule of enzyme
FAD
-
the fluorescence of FAD in oxidized wild-type enzyme is markedly temperature dependent, while the fluorescence of FAD in mutants C44S and C49S is independent of temperature
FAD
covalently bound to the protein
FAD
-
wild-type enzyme contains 1 FAD per subunit, mutant enzyme K37E has about 25% less bound FAD
FAD
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contains one noncovalently bound FAD per subunit
FAD
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contains one noncovalently bound FAD per subunit
FAD
-
1 FAD as prosthetic group per enzyme subunit
FAD
binding site amino acid sequence
FAD
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flavoenzyme, 1 FAD per enzyme subunit, functionally important
FAD
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prosthetic group, 1 FAD per enzyme subunit
FAD
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the cofactor is released from the enzyme with guanidine-HCl at concentration above 2 M forming inactive aggregates
FAD
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the enzyme contains 1 functionally important FAD per subunit
FAD
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tightly but noncovalently bound to the enzyme, the cofactor cycles between reduced and oxidized state during catalysis
FAD
contains a noncovalently but tightly attached FAD molecule
FAD
-
contains one FAD as a prosthetic group in each subunit
FAD
1.34 mol FAD per 1 mol of subunit of the enzyme
FAD
binding structure analysis
FAD
-
a flavoprotein, each monomer of 51000 Da binds one molecule of FAD
FAD
a single FAD is non-covalently arranged in each subunit
FAD
one FAD as a prosthetic group at each subunit
FAD
one FAD as a prosthetic group at each subunit, binding mode
FAD
one FAD as a prosthetic group at each subunit, binding structure analysis
flavin
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-
FMN
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-
NAD(P)H
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NADH is the preferred cofactor
NAD(P)H
-
NADPH and NADH are equally effective as cofactors
NAD(P)H
-
NADPH and NADH are utilized at similar rates for ubiquinone reduction
NAD+
-
-
NAD+
-
-
393971 , 393993 , 394003 , 394004 , 659101 , 672869 , 673943 , 674382 , 674759 , 675350 , 677161 , 691569 , 711099 , 764703
NAD+
Azotobacter agilis
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-
NAD+
-
highly specific for
NAD+
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highly specific for
NAD+
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the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
NAD+
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NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
NAD+
binding structure analysis
NAD+
binding structure analysis
NADH
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-
NADH
Starkeyomyces koorchalomoides
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-
NADH
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highly specific for
NADH
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highly specific for
NADH
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highly specific for
NADH
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highly specific for
NADH
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the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
NADH
has a preference for NADH as a coenzyme
NADH
high affinity for NADH, no activity with NADPH
NADH
binding structure analysis
NADP+
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NADPH
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-
NADPH
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oxidizes NADPH as efficiently as NADH
NADPH
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oxidizes NADPH as efficiently as NADH
ubiquinol
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-
additional information
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no activity with NADH
-
additional information
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no activity with NADPH
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additional information
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no activity with NADPH
-
additional information
-
enzyme contains 1 disulfide/dithiol per subunit
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additional information
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enzyme contains a redox-active disulfid, the cofactor cycles between reduced and oxidized state during catalysis, in the two-electron-reduced enzyme, the disulfide is reduced while the FAD cofactor is oxidized, in the four-electron.reduced enzyme, both redox centers are reduced
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additional information
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enzyme contains a redox-active disulfide, the cofactor cycles between reduced and oxidized state during catalysis
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additional information
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the enzyme contains 1 disulfide/dithiol per subunit
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additional information
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contains neither FMN nor FAD in the molecule
-
additional information
FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
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additional information
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FMN is not present in the recombinant enzyme as a cofactor. Does not use NADPH as the electron donor
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additional information
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unable to use NADP+ and NADPH
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additional information
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no cofactor: NADPH
-
additional information
no cofactor: NADPH
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additional information
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no cofactor: NADPH
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