Egbosimba EE: Evolutionary history of d-lactate dehydrogenases: A phylogenomic perspective on functional diversity in the FAD binding oxidoreductase/transferase type 4 family - ME () Citation Context ...equence has identified two Ldh genes, LdhA andLdhB, that are approximately 26 cM apart [16,17...
The structure of Erv2p, determined by X-ray crystallography to 1.5 Å resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) ...
Recently, mutations in electron transfer flavoprotein dehydrogenase (ETFDH) gene, encoding electron transfer flavoprotein:ubiquinone oxidoreductase (ETF:QO) have been reported to be the major causes of riboflavin-responsive MADD. To date, no studies have been performed to explore the functional impact ...
synthesis and evaluation of ()-dunnione and its ortho-quinone analogues as substrates for nad(p)hquinone oxidoreductase 1 (nqo1) 热度: Flavour development, analysis and perception in food and beverages-[1]-[J K Parker; J S Elmore; L Methven; D P Balagiannis] ...
Importantly, the sequence motifs in the transmembrane domain that are associated with the FAD and metal binding sites are not only present in Steap2 and Steap4 but also in Steap1, which lacks the N-terminal oxidoreductase domain. This strongly suggests that Steap1 harbors latent oxidoreductase ...
Cristescu ME, Egbosimba EE: Evolutionary history of d-lactate dehydrogenases: A phylogenomic perspective on functional diversity in the FAD binding oxidoreductase/transferase type 4 family. J Mol Evol 2009, 69 : 276-287. PubMed Abstract Publisher Full Text Return to textCristescu, M.E.,...
N-glycosylation affects deflavination and reconstitution of GMC-oxidoreductases.Bound FAD stabilizes the protein structure and increases thermal stability.FAD dissociation necessitates the movement of a surface loop in GMC-oxidoreductases.doi:10.1016/j.ijbiomac.2025.142470Su Ma...
Antley-Bixler syndrome (ABS), a steroidogenesic disorder, was attributed to deleterious mutations of the POR gene, encoding NADPH:cytochrome P450 oxidoreductase (CYPOR), the obligatory electron donor for microsomal cytochrome P450-(CYP) catalyzed reactions. CYPOR contains both FAD and FMN cofactors....
The structure of Erv2p, determined by X-ray crystallography to 1.5 脜 resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) ...
There is a region exhibiting a similarity of amino acid sequence near the carboxyl-terminal segment of each FAD-containing oxidoreductase. In this region, four amino acid residues-Thr, Ala, Gly, and Asp-are highly conserved. To determine the involvement of the four amino acid residues (Thr-...