A5041242705- Enzyme Structure and Function
- Amino Acid Enzymes and Metabolism
- Microbial Metabolic Engineering and Bioproduction
- Enzyme Catalysis and Immobilization
- Tryptophan and brain disorders
- Biochemical and Molecular Research
- Metabolism and Genetic Disorders
- Cancer Research and Treatments
- Protein Structure and Dynamics
- Biochemical Acid Research Studies
- Polyamine Metabolism and Applications
- Gut microbiota and health
- Stress Responses and Cortisol
- Metabolomics and Mass Spectrometry Studies
- Bacterial Genetics and Biotechnology
- Analytical Chemistry and Chromatography
- Hemoglobin structure and function
- Porphyrin Metabolism and Disorders
- Innovative Microfluidic and Catalytic Techniques Innovation
- Fluorine in Organic Chemistry
- Pharmacological Effects of Natural Compounds
- Poetry Analysis and Criticism
- Photosynthetic Processes and Mechanisms
- Carbohydrate Chemistry and Synthesis
- Enzyme Production and Characterization
University of Georgia
2025
University of Georgia
2015-2024
Regeneron (United States)
2016
Princeton University
2014
Piedmont Athens Regional
2014
Inserm
2008-2011
Ruijin Hospital
2011
Shanghai Institutes for Biological Sciences
2011
Chinese Academy of Sciences
2011
Shanghai Institute of Hypertension
2011
The DiscovEHR collaboration between the Regeneron Genetics Center and Geisinger Health System couples high-throughput sequencing to an integrated health care system using longitudinal electronic records (EHRs). We sequenced exomes of 50,726 adult participants in study identify ~4.2 million rare single-nucleotide variants insertion/deletion events, which ~176,000 are predicted result a loss gene function. Linking these data EHR-derived clinical phenotypes, we find associations supporting...
We demonstrated previously that genetic inactivation of tryptophanase is responsible for a dramatic decrease in biofilm formation the laboratory strain Escherichia coli S17-1. In present study, we tested whether biochemical inhibition tryptophanase, with competitive inhibitor oxindolyl-L-alanine, could affect polystyrene colonization by E. and other indole-producing bacteria. Oxindolyl-L-alanine inhibits, dose-dependent manner, indole production S17-1 grown LuriaBertani (LB) medium....
The efficiency of biocatalytic redox reactions catalyzed by alcohol dehydrogenases (ADHs) have been the subject considerable research recently. Two major challenges restricted their application in asymmetric synthesis until now. First all, most interesting substrates are either insoluble or sparingly soluble aqueous media, natural medium for enzymes. This drawback has overcome using non-aqueous media like organic solvents, ionic liquids, and supercritical carbon dioxide mono- biphasic...
The ability to control the substrate specificity and stereochemistry of enzymatic reactions is increasing interest in biocatalysis. As this review highlights, can be achieved through various means, including mutagenesis active site residues alteration physical variables such as temperature pressure well changing reaction medium. Although focus article on alcohol dehydrogenase reactions, each these techniques readily applied toward other enzyme classes, well.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThree-dimensional structure of tyrosine phenol-lyaseAlfred A. Antson, Tatyana V. Demidkina, Paul Gollnick, Zbigniew Dauter, Robert L. Von Tersch, John Long, Sergey N. Berezhnoy, S. Phillips, Emil H. Harutyunyan, and Keith WilsonCite this: Biochemistry 1993, 32, 16, 4195–4206Publication Date (Print):April 27, 1993Publication History Published online1 May 2002Published inissue 27 April...
Photosystem II (PSII) catalyzes the first of two photosynthetic reactions that convert sunlight into chemical energy. Native PSII is a supercomplex consisting core and light-harvesting chlorophyll proteins. Although structure has been resolved by x-ray crystallography, mechanism underlying its assembly poorly understood. Here, we report an immunophilin chloroplast thylakoid lumen required for accumulation in Arabidopsis thaliana. The immunophilin, FKBP20-2, belongs to FK-506 binding protein...
An enantioselective asymmetric reduction of phenyl ring-containing prochiral ketones to yield the corresponding optically active secondary alcohols was achieved with W110A alcohol dehydrogenase from Thermoanaerobacter ethanolicus (W110A TESADH) in Tris buffer using 2-propanol (30%, v/v) as cosolvent and cosubstrate. This concentration crucial not only enhance solubility hydrophobic substrates aqueous reaction medium, but also shift equilibrium direction. The resulting have S-configuration,...
The asymmetric reduction of benzylic and heteroaryl ketones to the corresponding (R)-alcohols using I86A Thermoanaerobacter ethanolicus alcohol dehydrogenase (I86A TeSADH) is described. This single amino acid mutation not only makes active site TeSADH able accommodate more sterically demanding substituents than those accommodated by wild-type TeSADH, but it also reverses substrate stereospecificity TeSADH. Detailed facts importance specialist readers are published as "Supporting...
Superoxide reductases (SORs) contain a novel square pyramidal ferrous [Fe(NHis)4(SCys)] site that rapidly reduces superoxide to hydrogen peroxide. Here we report extensive pulse radiolysis studies on recombinant two-iron SOR (2Fe-SOR) from Desulfovibrio vulgaris. The results support and elaborate our originally proposed scheme for reaction of the with [Coulter, E. D., Emerson, J. E., Kurtz, D. M., Jr., Cabelli, (2000) Am. Chem. Soc. 122, 11555−11556]. This consists second-order...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTEffects of substrate structure and temperature on the stereospecificity secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicusVan T. Pham Robert S. PhillipsCite this: J. Am. Chem. Soc. 1990, 112, 9, 3629–3632Publication Date (Print):April 1, 1990Publication History Published online1 May 2002Published inissue 1 April 1990https://doi.org/10.1021/ja00165a057RIGHTS & PERMISSIONSArticle Views591Altmetric-Citations75LEARN ABOUT THESE...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTTemperature-dependent enantiospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicusVan T. Pham, Robert S. Phillips, and Lars G. LjungdahlCite this: J. Am. Chem. Soc. 1989, 111, 5, 1935–1936Publication Date (Print):March 1, 1989Publication History Published online1 May 2002Published inissue 1 March 1989https://pubs.acs.org/doi/10.1021/ja00187a089https://doi.org/10.1021/ja00187a089research-articleACS PublicationsRequest...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInteractions of tryptophan synthase, tryptophanase, and pyridoxal phosphate with oxindolyl-L-alanine 2,3-dihydro-L-tryptophan: support for an indolenine intermediate in metabolismRobert S. Phillips, Edith Wilson Miles, Louis A. CohenCite this: Biochemistry 1984, 23, 25, 6228–6234Publication Date (Print):December 1, 1984Publication History Published online1 May 2002Published inissue 1 December...
To gel well: The asymmetric reduction of hydrophobic ketones by xerogel-immobilized W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus (TeSADH) in organic solvents affords their S-configured alcohols yields comparable with those achieved using the free enzyme, and, some cases, higher enantioselectivities. R=phenyl-ring-containing substituent.
Secondary alcohol dehydrogenase from<italic>Thermoanaerobacter ethanolicus</italic>was mutated at Trp-110, and mutant enzymes with high activity stereoselectivity for aromatic ketone reduction were identified.