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Information on EC 1.8.1.4 - dihydrolipoyl dehydrogenase and Organism(s) Arabidopsis thaliana

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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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Arabidopsis thaliana
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipoamide dehydrogenase, dihydrolipoamide dehydrogenase, dldh, l-protein, dihydrolipoyl dehydrogenase, nadh diaphorase, e3 component, lipdh, lipoyl dehydrogenase, nicotinamide adenine dinucleotide diaphorase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, lipoamide
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dehydrolipoate dehydrogenase
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DHLDH
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diaphorase
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dihydrolipoic dehydrogenase
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dihydrolipoyl dehydrogenase
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DLDH
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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
lipoamide dehydrogenase (NADH)
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lipoamide dehydrogenase2
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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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LPD1
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plastidial LPD1 encodes one of the two E3 isoforms found in the plastidial pyruvate dehydrogenase complex
NADH:lipoamide oxidoreductase
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ORF-E3
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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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
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r
DL-alpha-lipoamide + NADH
dihydrolipoamide + NAD+
show the reaction diagram
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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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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
activity of lipoamide dehydrogenase in isolated mitochondria is sensitive to arsenite, but not arsenate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
the enzyme is a key enzyme in oxidative metabolism
physiological function
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plastidial LPD expression quantitatively controls Arabidopsis arsenate sensitivity
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DLDH1_ARATH
507
0
53988
Swiss-Prot
Mitochondrion (Reliability: 1)
DLDH2_ARATH
507
0
53986
Swiss-Prot
Mitochondrion (Reliability: 1)
PLPD1_ARATH
623
0
66661
Swiss-Prot
Chloroplast (Reliability: 1)
PLPD2_ARATH
567
0
60145
Swiss-Prot
Chloroplast (Reliability: 1)
A0A654F7Y2_ARATH
623
0
66661
TrEMBL
Chloroplast (Reliability: 1)
A0A654F9D0_ARATH
507
0
53986
TrEMBL
Mitochondrion (Reliability: 1)
A0A178W162_ARATH
507
0
53988
TrEMBL
Mitochondrion (Reliability: 1)
A0A178VGZ6_ARATH
570
0
60757
TrEMBL
Chloroplast (Reliability: 1)
A0A5S9XED1_ARATH
623
0
66704
TrEMBL
Chloroplast (Reliability: 1)
A0A5S9WML4_ARATH
507
0
54028
TrEMBL
Mitochondrion (Reliability: 1)
A0A178VED5_ARATH
409
0
43838
TrEMBL
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 54000, about, sequence calculation, x * 55000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene lpd2, recombinant expression of GUS-linked enzyme in Arabidopsis thaliana ecotype Col-0 in cotyledons, rosette leaves and roots (in the cap of the established lateral roots, but not in the cap of the main roots) via transformation by Agrobacterium tumefaciens strain GV3101
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, W.; Chi, Y.; Taylor, N.L.; Lambers, H.; Finnegan, P.M.
Disruption of ptLPD1 or ptLPD2, genes that encode isoforms of the plastidial lipoamide dehydrogenase, confers arsenate hypersensitivity in Arabidopsis
Plant Physiol.
153
1385-1397
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Chen, W.; Taylor, N.L.; Chi, Y.; Millar, A.H.; Lambers, H.; Finnegan, P.M.
The metabolic acclimation of Arabidopsis thaliana to arsenate is sensitized by the loss of mitochondrial lipoamide dehydrogenase2, a key enzyme in oxidative metabolism
Plant Cell Environ.
37
684-695
2014
Arabidopsis thaliana (Q9M5K2), Arabidopsis thaliana
Manually annotated by BRENDA team