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1.8.1.4: dihydrolipoyl dehydrogenase

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

Word Map on EC 1.8.1.4

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

     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

Crystallization

Crystallization on EC 1.8.1.4 - dihydrolipoyl dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, X-ray diffraction structure determination and analysis, small-angle X-ray scattering of the enzyme in solution, measurements in 50 mM Tris buffer, pH 7.5, at 10°C, molecular docking and modeling
-
X-ray diffraction structure determination and analysis
crystals are grown from droplets of 0.002 ml of protein solution at 15 mg/ml and 0.002 ml of reservoir solution containing 10-20% polyethylene glycol 6000, 200 mM diammonium citrate, and 1 mM sodium azide
-
hanging drop vapour diffusion method
-
sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 7.45, 0.2 M MgCl2, 25% (w/v) PEG 3350 for the wild type enzyme and 1.6 M NaH2PO4/K2HPO4 pH 8.1 plus 2.5 M K2HPO4 for mutant enzyme D444V
-
alone or in complex with inhibitor N-(2,4-dichlorophenethyl)-2-[8-(2,4-dimethoxybenzoyl)-4-oxo-1-phenyl-1,3,8-triazaspiro-[4.5]decan-3-yl]acetamide, hanging drop vapor diffusion method, using 100 mM Tris (pH 8.5), 10 mM NaCl, 11% (w/v) polyethylene glycol 10000, and 15% (v/v) ethylene glycol
hanging drop vapour diffusion method
crystallization by dialysis
-
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
best results obtained by vapour diffusion method, three-dimensional structure at 2.8 A resolution
-
crystallized by hanging-drop vapor-diffusion method
-