Results 321 to 330 of about 810,832 (336)

Substrate specificity of pancreatic lipase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1968
Abstract 1. 1. The hydrolysis of esters of oleic acid by pancreatic lipase (glycerol-ester hydrolase, EC 3.1.1.3) depends on the nature of the alcohol. Two factors appear to influence the speed of the reaction: an inductive effect, and steric hindrance. 2. 2.
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Substrate specificity of strictosidine synthase

Bioorganic & Medicinal Chemistry Letters, 2006
Strictosidine synthase catalyzes a Pictet-Spengler reaction in the first step in the biosynthesis of terpene indole alkaloids to generate strictosidine. The substrate requirements for strictosidine synthase are systematically and quantitatively examined and the enzymatically generated compounds are processed by the second enzyme in this biosynthetic ...
McCoy, E, Galan , MC, O'Connor, SE
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Substrate specificity of muscle aldolase

Biochimica et Biophysica Acta, 1954
A study of the substrate specificity of rabbit muscle aldolase led to the following observations. 1. 1. Both the d and l isomers of glyceraldehyde-3-phosphate can be condensed with dihydroxylacetone phospahte, but the former appears to react much more rapidly than the latter. 2. 2. Tagatose-i, 6-diphosphate, which possesses a cis configuration
T C, TUNG, K H, LING, W L, BYRNE, H A, LARDY   +3 more
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Substrate specificity of adenovirus protease

Virus Research, 2002
The adenovirus protease, adenain is functionally required for virion uncoating and virion maturation and release from the infected cell. In addition to hydrolysis of precursor proteins at specific consensus sites, adenain has also been observed to cleave viral proteins at other sites. Here we re-examine the sequences in the consensus sites and also the
Angelique, Ruzindana-Umunyana, Lise, Imbeault, Joseph M, Weber   +2 more
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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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