1.8.1.4: dihydrolipoyl dehydrogenase

This is an abbreviated version!
For detailed information about dihydrolipoyl dehydrogenase, go to the full flat file.

Reaction

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

     1 Oxidoreductases

         1.8 Acting on a sulfur group of donors

             1.8.1 With NAD⁺ or NADP⁺ as acceptor

                1.8.1.4 dihydrolipoyl dehydrogenase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
17	Activating Compound
63885	AA Sequence
37	Application
1	CAS Registry Number
69	Cloned(Commentary)
340	Cofactor
14	Crystallization (Commentary)
625	Disease/ Diagnostics
3	Expression
73	General Information
3	General Stability
10	IC50 Value
102	Inhibitors
17	kcat/KM [mM/s]
32	Ki Value [mM]
282	KM Value [mM]
55	Localization
9	Metals/Ions
100	Molecular Weight [Da]
67	Natural Substrates/ Products (Substrates)
444	Organism
20	Pathway
169	PDB ID
57	pH Optimum
9	pH Range
2	pH Stability
6	pI Value
3	Posttranslational Modification
148	Protein Variants
93	Purification (Commentary)
15	Reaction
8	Reaction Type
247	Reference
1	Renatured (Commentary)
97	Source Tissue
76	Specific Activity [micromol/min/mg]
8	Storage Stability
431	Substrates and Products (Substrate)
123	Subunits
344	Synonyms
1	Systematic Name
28	Temperature Optimum [°C]
2	Temperature Range [°C]
22	Temperature Stability [°C]
98	Turnover Number [1/s]

Systematic Name

print visible entries

print all entries

Systematic Name on EC 1.8.1.4 - dihydrolipoyl dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Systematic Name Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

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].