Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity.
|Abstract||To this day, a significant proportion of the human genome remains devoid of functional characterization. In this study, we present evidence that the previously functionally uncharacterized product of the human DHRS10 gene is endowed with 17beta-HSD (17beta-hydroxysteroid dehydrogenase) activity. 17beta-HSD enzymes are primarily involved in the metabolism of steroids at the C-17 position and also of other substrates such as fatty acids, prostaglan ... [truncated at 450 characters in length]|
|Author||Lukacik, Petra; Keller, Brigitte; Bunkoczi, Gabor; et al|
|Subject||17-Hydroxysteroid Dehydrogenases Amino Acid Sequence Binding Sites Cell Line Crystallography, X-Ray Cytosol Gene Expression Humans Kinetics Ligands Models, Molecular Molecular Sequence Data NAD Organ Specificity Oxidation-Reduction Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Structural Homology, Protein chemistry genetics isolation and purification metabolism enzymology metabolism|
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
|Abstract||Glutamine synthetase (GS) catalyzes the ligation of glutamate and ammonia to form glutamine, with concomitant hydrolysis of ATP. In mammals, the activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine; there are a number of links between changes in GS activity and neurodegenerative disorders, such as Alzheimer's disease. In plants, because of its importance in the assimilation and re-assimilat ... [truncated at 450 characters in length]|
|Author||Krajewski, Wojciech W; Collins, Ruairi; Holmberg-Schiavone, Lovisa; et al|
|Subject||Adenosine Triphosphate Amino Acid Sequence Animals Apoenzymes Binding Sites Catalytic Domain Cloning, Molecular Crystallography, X-Ray Dogs Drug Design Drug Interactions Glutamate-Ammonia Ligase Herbicides Humans Hydrogen Bonding Kinetics Ligands Magnesium Models, Chemical Models, Molecular Molecular Sequence Data Pharmaceutical Preparations Protein Binding Protein Conformation Protein Structure, Tertiary Sequence Homology, Amino Acid Substrate Specificity Temperature metabolism pharmacology chemistry chemistry genetics isolation and purification metabolism chemical synthesis chemistry metabolism pharmacology chemical synthesis chemistry|
Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.
|Abstract||Human carbonyl reductase is a member of the short-chain dehydrogenase/reductase (SDR) protein superfamily and is known to play an important role in the detoxification of xenobiotics bearing a carbonyl group. The two monomeric NADPH-dependent human isoforms of cytosolic carbonyl reductase CBR1 and CBR3 show a sequence similarity of 85% on the amino acid level, which is definitely high if compared to the low similarities usually observed among othe ... [truncated at 450 characters in length]|
|Author||El-Hawari, Yasser; Favia, Angelo D; Pilka, Ewa S; et al|
|Subject||Alcohol Oxidoreductases Amino Acid Sequence Base Sequence Binding Sites Biocatalysis DNA Primers DNA, Complementary Humans Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Sequence Homology, Amino Acid Substrate Specificity chemistry genetics isolation and purification metabolism|
Expression and purification of recombinant human inward rectifier K+ (KCNJ) channels in Saccharomyces cerevisiae.
|Abstract||The inward rectifier family of potassium (KCNJ) channels regulate vital cellular processes including cell volume, electrical excitability, and insulin secretion. Dysfunction of different isoforms have been linked to numerous diseases including Bartter's, Andersen-Tawil, Smith-Magenis Syndromes, Type II diabetes mellitus, and epilepsy, making them important targets for therapeutic intervention. Using a family-based approach, we succeeded in expres ... [truncated at 450 characters in length]|
|Author||D'Avanzo, Nazzareno; Cheng, Wayland W L; Xia, Xiaobing; et al|
|Subject||Biochemistry Cloning, Molecular Humans Potassium Channels, Inwardly Rectifying Protein Transport Recombinant Proteins Saccharomyces cerevisiae Subcellular Fractions methods isolation and purification metabolism isolation and purification metabolism metabolism metabolism|
High-throughput production of human proteins for crystallization: the SGC experience.
|Abstract||Producing purified human proteins with high yield and purity remains a considerable challenge. We describe the methods utilized in the Structural Genomics Consortium (SGC) in Oxford, resulting in successful purification of 48% of human proteins attempted; of those, the structures of approximately 40% were solved by X-ray crystallography. The main driver has been the parallel processing of multiple (typically 9-20) truncated constructs of each tar ... [truncated at 450 characters in length]|
|Author||Savitsky, Pavel; Bray, James; Cooper, Christopher D O; et al|
|Subject||Amino Acid Sequence Animals Cell Line Cloning, Molecular Crystallography, X-Ray Genetic Vectors Genomics Humans Molecular Sequence Data Proteins Proteomics Recombinant Proteins genetics methods chemistry genetics metabolism methods chemistry isolation and purification metabolism|