Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase.
|Abstract||Human DHRS6 is a previously uncharacterized member of the short chain dehydrogenases/reductase family and displays significant homologies to bacterial hydroxybutyrate dehydrogenases. Substrate screening reveals sole NAD(+)-dependent conversion of (R)-hydroxybutyrate to acetoacetate with K(m) values of about 10 mm, consistent with plasma levels of circulating ketone bodies in situations of starvation or ketoacidosis. The structure of human DHRS6 w ... [truncated at 450 characters in length]|
|Author||Guo, Kunde; Lukacik, Petra; Papagrigoriou, Evangelos; et al|
|Subject||Amino Acid Motifs Amino Acid Sequence Animals Arginine Binding Sites Cloning, Molecular Crystallography, X-Ray Cytosol Dose-Response Relationship, Drug Exons Green Fluorescent Proteins Hela Cells Humans Hydrogen-Ion Concentration Hydroxybutyrate Dehydrogenase Kinetics Lipids Mitochondria Models, Molecular Molecular Sequence Data Oxidoreductases Phylogeny Protein Conformation Protein Folding Protein Structure, Tertiary Sequence Homology, Amino Acid Substrate Specificity Sulfates chemistry enzymology metabolism metabolism chemistry genetics chemistry metabolism chemistry chemistry|
Three-dimensional structure and enzymatic function of proapoptotic human p53-inducible quinone oxidoreductase PIG3.
|Abstract||Tumor suppressor p53 regulates the expression of p53-induced genes (PIG) that trigger apoptosis. PIG3 or TP53I3 is the only known member of the medium chain dehydrogenase/reductase superfamily induced by p53 and is used as a proapoptotic marker. Although the participation of PIG3 in the apoptotic pathway is proven, the protein and its mechanism of action were never characterized. We analyzed human PIG3 enzymatic function and found NADPH-dependent ... [truncated at 450 characters in length]|
|Author||Porté, Sergio; Valencia, Eva; Yakovtseva, Evgenia A; et al|
|Subject||Amino Acid Sequence Apoptosis Binding Sites Catalytic Domain Crystallography, X-Ray Humans Intracellular Signaling Peptides and Proteins Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed NADP Phylogeny Protein Structure, Quaternary Proto-Oncogene Proteins Reactive Oxygen Species Recombinant Proteins Sequence Homology, Amino Acid Tumor Suppressor Protein p53 Tyrosine physiology genetics chemistry genetics metabolism metabolism chemistry genetics metabolism metabolism chemistry genetics metabolism metabolism chemistry|
Superfamilies SDR and MDR: from early ancestry to present forms. Emergence of three lines, a Zn-metalloenzyme, and distinct variabilities.
|Abstract||Two large gene and protein superfamilies, SDR and MDR (short- and medium-chain dehydrogenases/reductases), were originally defined from analysis of alcohol and polyol dehydrogenases. The superfamilies contain minimally 82 and 25 genes, respectively, in humans, minimally 324 and 86 enzyme families when known lines in other organisms are also included, and over 47,000 and 15,000 variants in existing sequence data bank entries. SDR enzymes have one- ... [truncated at 450 characters in length]|
|Author||Jörnvall, Hans; Hedlund, Joel; Bergman, Tomas; et al|
|Subject||Acyl-CoA Dehydrogenase Butyryl-CoA Dehydrogenase Evolution, Molecular Humans Metalloproteins Phylogeny Protein Conformation Zinc chemistry classification genetics chemistry classification genetics chemistry classification genetics metabolism|