BIOMAT Database Logo BIOMAT Database Logo

The binding of trimethoprim to bacterial dihydrofolate reductase. 1981

D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers

UI MeSH Term Description Entries
D008727 Methotrexate An antineoplastic antimetabolite with immunosuppressant properties. It is an inhibitor of TETRAHYDROFOLATE DEHYDROGENASE and prevents the formation of tetrahydrofolate, necessary for synthesis of thymidylate, an essential component of DNA. Amethopterin,Methotrexate Hydrate,Methotrexate Sodium,Methotrexate, (D)-Isomer,Methotrexate, (DL)-Isomer,Methotrexate, Dicesium Salt,Methotrexate, Disodium Salt,Methotrexate, Sodium Salt,Mexate,Dicesium Salt Methotrexate,Hydrate, Methotrexate,Sodium, Methotrexate
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005583 Fourier Analysis Analysis based on the mathematical function first formulated by Jean-Baptiste-Joseph Fourier in 1807. The function, known as the Fourier transform, describes the sinusoidal pattern of any fluctuating pattern in the physical world in terms of its amplitude and its phase. It has broad applications in biomedicine, e.g., analysis of the x-ray crystallography data pivotal in identifying the double helical nature of DNA and in analysis of other molecules, including viruses, and the modified back-projection algorithm universally used in computerized tomography imaging, etc. (From Segen, The Dictionary of Modern Medicine, 1992) Fourier Series,Fourier Transform,Analysis, Cyclic,Analysis, Fourier,Cyclic Analysis,Analyses, Cyclic,Cyclic Analyses,Series, Fourier,Transform, Fourier
D013762 Tetrahydrofolate Dehydrogenase An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3. Dihydrofolate Dehydrogenase,Dihydrofolate Reductase,Folic Acid Reductase,Acid Reductase, Folic,Dehydrogenase, Dihydrofolate,Dehydrogenase, Tetrahydrofolate,Reductase, Dihydrofolate,Reductase, Folic Acid
D014295 Trimethoprim A pyrimidine inhibitor of dihydrofolate reductase, it is an antibacterial related to PYRIMETHAMINE. It is potentiated by SULFONAMIDES and the TRIMETHOPRIM, SULFAMETHOXAZOLE DRUG COMBINATION is the form most often used. It is sometimes used alone as an antimalarial. TRIMETHOPRIM RESISTANCE has been reported. Proloprim,Trimpex
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Nuclear magnetic resonance studies of the binding of trimethoprim to dihydrofolate reductase.
September 1979, Biochemistry,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Dynamics of trimethoprim bound to dihydrofolate reductase.
June 1988, Proceedings of the National Academy of Sciences of the United States of America,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Trimethoprim binding to Lactobacillus casei dihydrofolate reductase: a 13C NMR study using selectively 13C-enriched trimethoprim.
April 1986, Biochemistry,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Trimethoprim binding to bacterial and mammalian dihydrofolate reductase: a comparison by proton and carbon-13 nuclear magnetic resonance.
November 1983, Biochemistry,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase.
January 2016, Biochemistry,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Methotrexate binding to dihydrofolate reductase.
July 1980, Nature,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
The charge state of trimethoprim bound to Lactobacillus casei dihydrofolate reductase.
August 1981, FEBS letters,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Trimethoprim binds in a bacterial mode to the wild-type and E30D mutant of mouse dihydrofolate reductase.
October 1991, The Journal of biological chemistry,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Multiple ligand-binding modes in bacterial R67 dihydrofolate reductase.
March 2005, Journal of computer-aided molecular design,
D J Baker, and C R Beddell, and J N Champness, and P J Goodford, and F E Norrington, and D R Smith, and D K Stammers
Protonated state of methotrexate, trimethoprim, and pyrimethamine bound to dihydrofolate reductase.
October 1983, Archives of biochemistry and biophysics,
Copied contents to your clipboard!