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Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P11959

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EC Tree
IUBMB Comments
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein .
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Geobacillus stearothermophilus
UNIPROT: P11959
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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipoamide dehydrogenase, dihydrolipoamide dehydrogenase, dldh, dihydrolipoyl dehydrogenase, l-protein, nadh diaphorase, e3 component, lipdh, lipoyl dehydrogenase, nicotinamide adenine dinucleotide diaphorase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrolipoamide dehydrogenase
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dehydrogenase, lipoamide
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dehydrolipoate dehydrogenase
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DHLDH
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diaphorase
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dihydrolipoamide dehydrogenase
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dihydrolipoamide dehydrogenase E3
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common component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
dihydrolipoic dehydrogenase
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dihydrolipoyl dehydrogenase
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DLDH
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-
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E3
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-
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E3 component of 2-oxoglutarate dehydrogenase complex
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-
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E3 component of acetoin cleaving system
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E3 component of alpha keto acid dehydrogenase complexes
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E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
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E3 component of pyruvate complex
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E3 lipoamide dehydrogenase
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Glycine cleavage system L protein
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Glycine oxidation system L-factor
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LDP-Glc
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LDP-Val
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lipoamide dehydrogenase (NADH)
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lipoamide oxidoreductase (NADH)
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lipoamide reductase
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lipoate dehydrogenase
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lipoic acid dehydrogenase
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lipoyl dehydrogenase
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LPD
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LPD-GLC
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LPD-VAL
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NADH:lipoamide oxidoreductase
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ORF-E3
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system ({AminoAcid/GlyCleave} for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-18-7
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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
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
tellurite + NADH
NAD+ + ?
show the reaction diagram
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?
dihydrolipoamide + NAD+
lipoamide + NADH
show the reaction diagram
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?
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
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?
additional information
?
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + NAD+
lipoamide + NADH + H+
show the reaction diagram
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-
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r
additional information
?
-
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the enzyme is a component of the three 2-oxoacid dehydrogenase complexes oxidizing pyruvate, 2-oxoglutarate, and the branched-chain 2-oxo acids
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
a single FAD is non-covalently arranged in each subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Guanidine-HCl
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4°C: 50% inactivation at 1.0 M, complete inactivation at 1.6 M, reversible
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Guanidine-HCl
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4°C: activates the enzyme 2.5fold at 0.2 M
KCl
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4°C: activates the enzyme at concentrations below 1 M
NaCl
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4°C: activates the enzyme at concentrations below 1 M
additional information
-
no activation by urea
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
dihydrolipoamide dehydrogenase (LipDH) transfers two electrons from dihydrolipoamide to NAD+ mediated by FAD. Since this reaction is the final step of a series of catalytic reaction of pyruvate dehydrogenase multi-enzyme complex (PDC), LipDH is a key enzyme to maintain the fluent metabolic flow
additional information
conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DLDH1_GEOSE
470
0
49356
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
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x * 54000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 54000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray diffraction structure determination and analysis
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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the enzyme unfolds irreversibly at heat treatment higher than 65°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Q column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase multienzyme complex, expression in Escherichia coli
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inactivation of the enzyme by guanidine-HCl is reversible by its removal
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
shows NADH-dependent tellurite reductase activity in vitro
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borges, A.; Hawkins, C.F.; Packman, L.C.; Perham, R.N.
Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
Eur. J. Biochem.
194
95-102
1990
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Carothers, D.J.; Pons, G.; Patel, M.S.
Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases
Arch. Biochem. Biophys.
268
409-425
1989
Ascaris suum, Azotobacter vinelandii, Bacillus subtilis, Bos taurus, Escherichia coli, Geobacillus stearothermophilus, Halobacterium salinarum, Homo sapiens, Pisum sativum, Pseudomonas aeruginosa, Pseudomonas putida, Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces pastorianus, Sus scrofa
Manually annotated by BRENDA team
Hiromasa, Y.; Meno, K.; Aso, Y.
Denaturation of the Bacillus stearothermophilus dihydrolipoamide dehydrogenase in the presence of guanidine-HCl at low temperature
J. Fac. Agric. Kyushu Univ.
47
387-394
2003
Geobacillus stearothermophilus
-
Manually annotated by BRENDA team
Nishimoto, E.; Aso, Y.; Koga, T.; Yamashita, S.
Thermal unfolding process of dihydrolipoamide dehydrogenase studied by fluorescence spectroscopy
J. Biochem.
140
349-357
2006
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Castro, M.E.; Molina, R.; Diaz, W.; Pichuantes, S.E.; Vasquez, C.C.
The dihydrolipoamide dehydrogenase of Aeromonas caviae ST exhibits NADH-dependent tellurite reductase activity
Biochem. Biophys. Res. Commun.
375
91-94
2008
Aeromonas caviae, Escherichia coli, Geobacillus stearothermophilus (P11959), Geobacillus stearothermophilus, Zymomonas mobilis (P50970), Zymomonas mobilis, Streptococcus pneumoniae (Q8VPK7), Streptococcus pneumoniae
Manually annotated by BRENDA team
Fukamichi, T.; Nishimoto, E.
Conformational change near the redox center of dihydrolipoamide dehydrogenase induced by NAD+ to regulate the enzyme activity
J. Fluoresc.
25
577-583
2015
Geobacillus stearothermophilus (P11959)
Manually annotated by BRENDA team