Results 291 to 300 of about 660,873 (335)
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The Substrate Specificity of Sirtuins
Annual Review of Biochemistry, 2016Sirtuins are NAD+-dependent enzymes universally present in all organisms, where they play central roles in regulating numerous biological processes. Although early studies showed that sirtuins deacetylated lysines in a reaction that consumes NAD+, more recent studies have revealed that these enzymes can remove a variety of acyl-lysine modifications ...
Cynthia Wolberger +4 more
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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 ...
John T. Capecchi, Gordon Marc 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.
D.B. Coult +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 ...
Devidayal Munjal, Noel R. Rose
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Substrate specificities of tobacco chitinases
The Plant Journal, 1998Ten tobacco chitinases (1,4-N-acetyl-beta-D-glucosaminide glycanhydrolase, EC 3.2.1.14) were purified from tobacco leaves hypersensitively reacting to tobacco mosaic virus. The 10 enzymes, which belong to five distinct structural classes of plant chitinases, were incubated with several potential substrates such as chitin, a beta-1,4 N-acetyl-D ...
Bernard Fritig +3 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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The substrate specificity of tocopherol cyclase
Bioorganic & Medicinal Chemistry, 1996The substrate specificity of the enzyme tocopherol cyclase from the blue-green algae Anabaena variabilis (Cyanobacteria) was investigated with 11 substrate analogues revealing the significance of three major recognition sites: (i) the OH group at C(1) of the hydroquinone, (ii) the (E) configuration of the double bond, and (iii) the length of the ...
Wolf-Dietrich Woggon +4 more
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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 ...
Alexander Blinkovsky +5 more
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Substrate specificity of polyphenol oxidase
Critical Reviews in Biochemistry and Molecular Biology, 2020The ubiquitous type-3 copper enzyme polyphenol oxidase (PPO) has found itself the subject of profound inhibitor research due to its role in fruit and vegetable browning and mammalian pigmentation. The enzyme itself has also been applied in the fields of bioremediation, biocatalysis and biosensing.
Ivanhoe K. H. Leung +1 more
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Engineering substrate specificity
Current Opinion in Structural Biology, 1991Site-directed mutagenesis of amino acids in the active site of an enzyme can yield mutant proteins with dramatically altered substrate specificity. In the past year, several enzymes have been successfully engineered with desired changes in specificity.
David A. Agard, Charles B. Wilson
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