Results 231 to 240 of about 30,996 (262)

Computation of enzyme-substrate specificity

Biochemistry, 1981
The present study reports the development of a new procedure for teh theoretical computation of enzyme-substrate specificities. The immediate goal has been to identify experimental data with which computations may be effectively compared, examine the underlying theoretical principles, and demonstrate feasibility.
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Substrate Specificity in Thiol Dioxygenases

Biochemistry, 2019
Thiol dioxygenases make up a class of ferrous iron-dependent enzymes that oxidize thiols to their corresponding sulfinates. X-ray diffraction structures of cysteine-bound cysteine dioxygenase show how cysteine is coordinated via its thiolate and amine to the iron and oriented correctly for O atom transfer.
Sekotilani Aloi, Casey G. Davies, P. Andrew Karplus, Sigurd M. Wilbanks, Guy N. L. Jameson   +4 more
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Substrate specificity of formylglycinamidine synthetase

Biochemistry, 1986
Formylglycinamidine ribonucleotide (FGAM) synthetase, which catalyzes the conversion of formylglycinamide ribonucleotide (FGAR), glutamine, and ATP to FGAM, ADP, glutamate, and Pi, has been purified to homogeneity (sp act. 0.20 mumol min-1 mg-1) from chicken liver by an alternative procedure to that of Buchanan et al. [Buchanan, J.
F J, Schendel, J, Stubbe
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Substrate specificity in pectin synthesis

Biochemical and Biophysical Research Communications, 1966
Abstract Particulate preparations from higher plants incorporate galacturonic acid from UDP-galacturonate into a “pectin-like” material. The enzymatic reaction is fairly specific for UDP-GalUA although some incorporation of TDP-GalUA was observed with tomato particles, and a slight incorporation of CDP-GalUA with mung bean particles.
T Y, Lin, A D, Elbein, J C, Su
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Substrate Specificity of Alcohol Dehydrogenases

1993
Alcohol dehydrogenases have important physiological fonctions. Thus, it is important to determine the substrate specificities of these enzymes. Usually, a variety of substrates are chosen for a survey, and the most reactive substrates are identified by steady-state kinetic methods.
B V, Plapp, D W, Green, H W, Sun, D H, Park, K, Kim   +4 more
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Substrate Specificities of Acid Kininogenases

1979
Two kinin forming enzymes were extracted from bovine spleen and separated from cathepsin B1 and B2 by DEAE-Cellulose chromatography. Since these catheptic kininogenases were found to release kinins from kininogens at acidic pH's, these were named acid kininogenase I and II.
K, Yamafuji, M, Takeishi
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Substrate specificity of prostatic phosphomonoesterase

Archives of Biochemistry and Biophysics, 1964
Abstract Prostatic phosphomonoesterase was found to be much less active in removing monoesterified phosphate groups from oligonucleotides than from mononucleotides. The activity of the enzyme decreased with increasing chain length from the mono- to the tetranucleotides.
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Substrate Specificity of Peroxidase

Science, 1955
R R, FERGUSSON, B, CHANCE
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Integrative oncology: Addressing the global challenges of cancer prevention and treatment

Ca-A Cancer Journal for Clinicians, 2022
Jun J Mao,, Msce, Lorenzo Cohen, Karen M Mustian   +2 more
exaly  

Tracking E2-specific substrates

Nature Chemical Biology
Jones, HBL, Damianou, A, Kessler, B
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