Results 261 to 270 of about 33,198 (306)
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Substrate specificity of pullulanase
Archives of Biochemistry and Biophysics, 1970Abstract Action of pullulanase from Aerobacter aerogenes has been tested on a number of starch oligosaccharides. Hydrolysis is confined to cleavage of α-1 → 6-interchain links between oligosaccharide chains containing a minimum of two glucose units per chain.
M, Abdullah, D, French
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Substrate specificity of pyroglutamylaminopeptidase
Journal of Medicinal Chemistry, 1985Three synthetic peptides (compounds 4-6) were tested as substrates of pyroglutamylaminopeptidase. In addition, inhibition of the hydrolysis of these substrates by compounds 8 and 9 was also examined. The enzyme does not appreciably catalyze the hydrolysis of peptides with six-membered ureido rings at the amino terminus, but it tolerates well a five ...
J T, Capecchi, G M, Loudon
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Substrate specificity of caeruloplasmin. Phenylalkylamine substrates
Biochemical Pharmacology, 1974Abstract Several phenylalkylamines have been examined as substrates for the copper-containing oxidase caeruloplasmin and it has been shown that the compounds most readily oxidized by this enzyme are those which contain a 3,4-dioxygenation pattern in the aromatic ring.
B C, Barrass +3 more
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Substrate specificity of a human-specific esterase
Analytical Biochemistry, 1973Abstract A human species-specific esterase has been identified in tissues, cell cultures, and urine. It is the most slowly migrating (i.e., cathodal) of the esterase isoenzymes in agarose electrophoresis; it is not a choline estrase, a pseudocholine esterase, an acetyl phenylalanine-3-naphthyl esterase or N -benzoyl-arginine-3-naphthyl esterase ...
D, Munjal, N R, Rose
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Substrate specificity of Streptomyces transglutaminases
Applied Biochemistry and Biotechnology, 2007Transglutaminase (TGase) is a multifunctional enzyme vital for many physiologic processes, such as cell differentiation, tissue regeneration, and plant pathogenicity. The acyl transfer function of the enzyme can activate primary amines and, consequently, attach them onto a peptidyl glutamine, a reaction important for various in vivo and in vitro ...
James, Langston +5 more
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Substrate specificity of neuraminidases
The Histochemical Journal, 1973This presentation is a brief description of neuraminidases and is mainly concerned with the substrate specificity of these enzymes. From the observed great differences in substrate specificity it is clear that we are dealing not with one enzyme called neuraminidase but with a variety of enzymes named neuraminidases.
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Substrate specificity of strictosidine synthase
Bioorganic & Medicinal Chemistry Letters, 2006Strictosidine 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 ascorbate oxidase
Biochemical and Biophysical Research Communications, 1976Abstract Ascorbate oxidase oxidizes leuco 2, 6-dichloroindophenol to the blue quinoid dye and produces spectral changes in the UV spectra of certain substituted polyhydric and amino phenols at pH 5.7. The new peaks produced by the addition of enzyme to the dichlorohydroquinones (2,5 and 2,6) and hydroxyhydroquinone correspond to the respective p ...
J, Dayan, C R, Dawson
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Substrate specificity of squalene synthetase
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 198022 artificial homologues of farnesyl pyrophosphate were examined for the reactivity as substrate for squalene synthetase of pig liver microsomes. 16 of the homologues were found to be reactive to give corresponding squalene-like products. Extention of the omega-terminal of the carbon chain of farnesyl pyrophosphate is acceptable to the enzyme at least ...
T, Koyama, K, Ogura, S, Seto
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Substrate specificity of adenovirus protease
Virus Research, 2002The 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 +2 more
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