Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11→q22 region of chromosome 5. Bacterial species possess distinct DHFR enzymes, but mammalian DHFRs are highly similar.
Chemical biology is a scientific discipline spanning the fields of chemistry and biology. The discipline involves the application of chemical techniques, analysis, and often small molecules produced through synthetic chemistry, to the study and manipulation of biological systems. In contrast to biochemistry, which involves the study of the chemistry of biomolecules and regulation of biochemical pathways within and between cells, chemical biology deals with chemistry applied to biology.
Stephen B. H. Kent is a chemistry professor at the University of Chicago. While professor at the Scripps Research Institute in the early 1990s he pioneered modern ligation methods for the total chemical synthesis of proteins. He was the inventor of native chemical ligation together with his student Philip Dawson. His laboratory experimentally demonstrated the principle that chemical synthesis of a protein's polypeptide chain using mirror-image amino acids after folding results in a mirror-image protein molecule which, if an enzyme, will catalyze a chemical reaction with mirror-image stereospecificity. At the University of Chicago Kent and his junior colleagues pioneered the elucidation of protein structures by quasi-racemic & racemic crystallography.
Christopher Abell was a British biological chemist. He was Professor of Biological Chemistry at the Department of Chemistry of the University of Cambridge and Todd-Hamied Fellow of Christ's College, Cambridge. On his 2016 election to the Royal Society, the society described his research as having "changed the face of drug discovery."
Ronald T. Raines is an American chemical biologist. He is the Roger and Georges Firmenich Professor of Natural Products Chemistry at the Massachusetts Institute of Technology. He is known for using ideas and methods of physical organic chemistry to solve important problems in biology.
Duilio Arigoni was a Swiss chemist and Emeritus Professor at ETH Zurich. He worked on the biosynthetic pathways of many organic natural substances.
Dieter Seebach is a German chemist known for his synthesis of biopolymers and dendrimers, and for his contributions to stereochemistry. He was born on 31 October 1937 in Karlsruhe. He studied chemistry at the University of Karlsruhe (TH) under the supervision of Rudolf Criegee and at Harvard University with Elias Corey finishing in 1969. After his habilitation he became professor for organic chemistry at the University of Giessen. After six years he was appointed professor at the ETH Zurich where he worked until he retired in 2003.
In enzymology, bornyl diphosphate synthase (BPPS) is an enzyme that catalyzes the chemical reaction
In enzymology, a dihydrofolate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a tetrahydrofolate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, an aristolochene synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a germacrene-A synthase is an enzyme that catalyzes the chemical reaction
Absinthin is a naturally produced triterpene lactone from the plant Artemisia absinthium (Wormwood). It constitutes one of the most bitter chemical agents responsible for absinthe's distinct taste. The compound shows biological activity and has shown promise as an anti-inflammatory agent, and should not to be confused with thujone, a neurotoxin also found in Artemisia absinthium.
Geosmin synthase or germacradienol-geosmin synthase designates a class of bifunctional enzymes that catalyze the conversion of farnesyl diphosphate (FPP) to geosmin, a volatile organic compound known for its earthy smell. The N-terminal half of the protein catalyzes the conversion of farnesyl diphosphate to germacradienol and germacrene D, followed by the C-terminal-mediated conversion of germacradienol to geosmin. The conversion of FPP to geosmin was previously thought to involve multiple enzymes in a biosynthetic pathway.
5-epiaristolochene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -5-epiaristolochene-forming). This enzyme catalyses the following chemical reaction
(-)-alpha-terpineol synthase (EC 4.2.3.111) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, (-)-alpha-terpineol-forming). This enzyme catalyses the following chemical reaction
Photoactivated peptides are modified natural or synthetic peptides the functions of which can be activated with light. This can be done either irreversibly or in a reversible way. Caged peptides which contain photocleavable protecting groups belong to irreversibly activated peptides. Reversible activation/deactivation of peptide function are achieved by incorporation photo-controllable fragments in the side chains or in the backbone of peptide templates to get the photo-controlled peptides, which can reversibly change their structure upon irradiation with light of different wavelength. As the consequence, the properties, function and biological activity of the modified peptides can be controlled by light. Since light can be directed to specific areas, such peptides can be activated only at targeted sites. Azobenzenes, and diarylethenes can be used as the photoswitches. For therapeutic use, photoswitches with longer wavelengths or the use of two-photon excitation are required, coupled with improved methods for peptide delivery to live cells.
Sandeep Verma is an Indian bioorganic chemist and chemical biologist, and a Professor in the Department of Chemistry at the Indian Institute of Technology, Kanpur (IITK). At IITK, he heads Sandeep Verma's Research Group in the areas of ordered peptide assemblies, metal-mediated nanoscale systems, programmable soft matter for neuronal regeneration, novel antimicrobials, and small molecule-stem cell modulation. He is an elected fellow of the Indian National Science Academy (INSA), the Indian Academy of Sciences and the National Academy of Sciences, India. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 2010, for his contributions to Chemical Sciences.
Dan Thomas Major is a Professor of Chemistry at Bar Ilan University specializing in Computational Chemistry.
Cyclodipeptide synthases (CDPSs) are a newly defined family of peptide-bond forming enzymes that are responsible for the ribosome-independent biosynthesis of various cyclodipeptides, which are the precursors of many natural products with important biological activities. As a substrate for this synthesis, CDPSs use two amino acids activated as aminoacyl-tRNAs (aa-tRNAs), therefore diverting them from the ribosomal machinery. The first member of this family was identified in 2002 during the characterization of the albonoursin biosynthetic pathway in Streptomyces noursei. CDPSs are present in bacteria, fungi, and animal cells.
