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Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I3D1
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1.8.1.4 dihydrolipoyl dehydrogenaseIUBMB 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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Word Map
- 1.8.1.4
-
multienzyme
- fad
- acetyltransferase
- dehydrogenases
- alpha-ketoglutarate
- flavin
-
branched-chain
- flavoproteins
- transacetylase
- thioredoxin
-
azotobacter
- vinelandii
- thiamin
-
subcomplexes
-
alpha-keto
- acidosis
- alpha-ketoacids
- succinyltransferase
-
mercuric
-
flavoenzymes
- 2-oxoacids
- trypanothione
- friedreich
-
1.2.4.1
-
subunit-binding
-
two-electron
-
radiofrequency
- medicine
-
ketoacids
- degradation
-
ashkenazi
-
t-proteins
-
myenteric
- analysis
- drug development
- diagnostics
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, lipoamide
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-
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dehydrolipoate dehydrogenase
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DHLDH
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diaphorase
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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
E3
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E3 component of 2-oxoglutarate dehydrogenase complex
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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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DLDH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
Biosynthesis of secondary metabolites, Citrate cycle (TCA cycle), Glycine, serine and threonine metabolism, Glycolysis / Gluconeogenesis, Lysine degradation, Microbial metabolism in diverse environments, Propanoate metabolism, Pyruvate metabolism, Tryptophan metabolism, Valine, leucine and isoleucine degradation
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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
9001-18-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + NAD+
lipoamide + NADH + H+
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-
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r
methylene blue + NADH + H+
reduced methylene blue + NAD+
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-
-
?
pyocyanin + NADH + H+
reduced pyocyanin + NAD+
pyocyanin is reported to stimulate respiration
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-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
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-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
PCA, the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling. Enzyme LpdG residues Val191 and Ile192 do not sterically hinder PCA frombinding to LpdG
-
-
?
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
the precursor for all biological phenazines in Pseudomonas aeruginosa, promotes anaerobic energy generation by redox cycling
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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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?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
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-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
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-
?
additional information
?
-
phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. PCA and pyocyanin reduction by the purified complexes required all substrates and cofactors
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + NAD+
lipoamide + NADH + H+
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-
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r
phenazine-1-carboxylic acid + NADH + H+
reduced phenazine-1-carboxylic acid + NAD+
by cell lysate
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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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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphenyleneiodonium
an inhibitor of flavoproteins and heme-containing proteins, effectively inhibits phenazine reduction in vitro
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
physiological function
LpdG, not LpdV and Lpd3, is the primary DLDH of the Pseudomonas aeruginosa PA14 pyruvate dehydrogenase, and is the enzymatically relevant DLDH for both pyruvate and 2-oxoglutarate dehydrogenase
additional information
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
additional information
purification of an NADH:PCA or NADPH:PCA oxidoreductase, active with phenazine-1-carboxylic acid and other phenazines, from Pseudomonas aeruginosa cell lysate is not successful. Structural analysis of LpdG, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in apoform, and in complexes with Nad+ and NADH, X-ray diffraction structure determination and analysis at 1.35-1.79 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I192G
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
V191Y
site-directed mutagenesis, the mutant is active with phenazine-1-carboxylic acid
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration. Purification of native pyruvate and2-oxoglutarate dehydrogenase complexes from strain PA14 by hydroxyapatite chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene lpd3, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene lpdG, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene lpdV, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
enzyme is surface-exposed and contributes to survival of Pseudomonas aeruginosa in human serum. Enzyme binds the four human plasma proteins, Factor H, factor H-like protein-1, complement factor H-related protein 1, and plasminogen. Factor H contacts the enzyme via short consensus repeats 7 and 18-20. Factor H, factor H-like protein-1, and plasminogen when bound to enzyme are functionally active. Bacterial survival is reduced when the enzyme is blocked on the surface prior to challenge with human serum. Similarly, bacterial survival is reduced up to 84% when the bacteria are challenged with complement active serum depleted of factor H, factor H-like protein-1, and complement factor H-related protein 1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sokatch, J.R.
Purification of branched-chain keto acid dehydrogenase and lipoamide dehydrogenase-valine from Pseudomonas
Methods Enzymol.
166
342-350
1988
Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas putida PpG2
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
Hallstroem, T.; Moergelin, M.; Barthel, D.; Raguse, M.; Kunert, A.; Hoffmann, R.; Skerka, C.; Zipfel, P.F.
Dihydrolipoamide dehydrogenase of Pseudomonas aeruginosa is a surface-exposed immune evasion protein that binds three members of the factor H family and plasminogen
J. Immunol.
189
4939-4950
2012
Pseudomonas aeruginosa (Q9I3D1), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9I3D1)
Glasser, N.R.; Wang, B.X.; Hoy, J.A.; Newman, D.K.
The pyruvate and alpha-ketoglutarate dehydrogenase complexes of Pseudomonas aeruginosa catalyze pyocyanin and phenazine-1-carboxylic acid reduction via the subunit dihydrolipoamide dehydrogenase
J. Biol. Chem.
292
5593-5607
2017
Pseudomonas aeruginosa (A0A0H2Z9F5), Pseudomonas aeruginosa (A0A0H2ZB32), Pseudomonas aeruginosa (A0A0H2ZHZ0), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2Z9F5), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZB32), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZHZ0)
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