Results 341 to 350 of about 10,438,012 (377)
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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.
Mark-Anthony McLarin +1 more
semanticscholar +4 more sources
Substrate Specificity of Mycodextranase
Nature, 1966MYCODEXTRAN (nigeran) is an unbranched polysaccharide composed of a regular alternating sequence of α–(1rarr;3) and α–(1→4) linked glucopyranosyl units. It is produced in the mycelia of various species of moulds1. Reese and Mandels have recently reported2 the isolation and partial purification of an inducible glucanase (mycodextranase) produced in the ...
S. Hasegawa +3 more
openaire +3 more sources
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.
Dexter French, Mukhtar Abdullah
openaire +3 more sources
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
openaire +3 more sources
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
openaire +3 more sources
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
openaire +3 more sources
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
openaire +2 more sources
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
openaire +3 more sources