protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase
Glycine, serine and threonine metabolism
Valine, leucine and isoleucine degradation
Pig heart lipoamide dehydrogenase: solvent equilibrium and kinetic isotope effects.
Multifunctionality of lipoamide dehydrogenase: activities of chemically trapped monomeric and dimeric enzymes.
Proton nuclear magnetic resonance investigation of the mechanism of flavin C-4a adduct formation induced by oxidized nicotinamide adenine dinucleotide binding to monoalkylated pig heart lipoamide dehydrogenase.
Structural relationship between glutathione reductase and lipoamide dehydrogenase.
X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method.
X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques.
NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals.
Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes.
The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii.
Mechanisms of generation of oxygen radicals and reductive mobilization of ferritin iron by lipoamide dehydrogenase.
Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase.
Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: role of flavin and the reactive disulfide groups.
Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes.
Lipoamide dehydrogenase from Azotobacter vinelandii. The role of the C-terminus in catalysis and dimer stabilization.
pH dependent kinetic studies of lipoamide dehydrogenase catalysis.
Characterization of two site-specifically mutated human dihydrolipoamide dehydrogenases (His-452----Gln and Glu-457----Gln).
The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution.
One-electron reduction of vanadium(V) by flavoenzymes/NADPH.
Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescens at 2.8 A resolution. Analysis of redox and thermostability properties.
The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex.
Flavoprotein structure and mechanism. 5. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design.
Chemical modification of the N-10 ribityl side chain of flavins. Effects on properties of flavoprotein disulfide oxidoreductases.
Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis.
2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain.
Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis.
Effect of increasing methylation on the ability of methylene blue to cause diaphorase-catalysed oxidation of NADH.
Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins.
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies.
FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli.
Electrocatalytic reduction of lipoic acid and electroenzymatic reduction of NAD(P)(+) for integrated dehydrogenase biosensors.
Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis.
2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity.
Diaphorase catalyzed biotransformation of RDX via N-denitration mechanism.
The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis.
Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein.
Crystal structure and functional analysis of lipoamide dehydrogenase from Mycobacterium tuberculosis.
Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.
This enzyme is one of the component of the pyruvate dehydrogenase multienzyme complex which is composed of dihydrolipoamide acetyltransferase(E1), pyruvate decarboxylase(E2), and dihydrolipoamide dehydrogenase(E3). Moreover, it is homologous to the L protein of glycine cleavage system (M00163 in EzCatDB). According to the literature [36], this enzyme catalyzes the following reactions: (A) Hydride transfer from NADH to FAD, giving reduced flavin (FADH2): (B) Electron transfer from FADH2 to the redox-active disulfide bond (Cys-Cys), giving the oxidized flavin (FAD): (C) Electron transfer from the active site cysteine residues to lipoamide substrate, giving dihyrolipoamide and the disulfide bond of the cysteine residues. In the so-called reductive half-reaction, the reactions, (A) and (B), occur. In the so-called oxidative half-reaction, the reaction, (C), occurs subsequently.