Results 301 to 310 of about 810,832 (336)

Substrate specificity and protein stability drive the divergence of plant-specific DNA methyltransferases. [PDF]

Sci Adv
Jiang J, Gwee J, Fang J, Leichter SM, Sanders D, Ji X, Song J, Zhong X.   +7 more
europepmc   +1 more source

Impact of the changes in substrate specificity of herpes simplex virus 1 protein kinase Us3 on viral infection <i>in vitro</i> and <i>in vivo</i>. [PDF]

J Virol
Shio S, Kato A, Kawasaki J, Takeshima K, Maruzuru Y, Koyanagi N, Harima H, Kawaguchi Y.   +7 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Substrate specificity of caeruloplasmin. Phenylalkylamine substrates

Biochemical Pharmacology, 1974
Abstract 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, D B, Coult, P, Rich, K J, Tutt   +3 more
openaire   +2 more sources

Substrate Specificity of Mycodextranase

Nature, 1966
MYCODEXTRAN (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 ...
J H, Nordin, S, Hasegawa, F, Smith, S, Kirkwood   +3 more
openaire   +2 more sources

Substrate specificity of pullulanase

Archives of Biochemistry and Biophysics, 1970
Abstract 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
openaire   +2 more sources

Substrate specificity of pyroglutamylaminopeptidase

Journal of Medicinal Chemistry, 1985
Three 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
openaire   +2 more sources

The Substrate Specificity of Sirtuins

Annual Review of Biochemistry, 2016
Sirtuins are NAD + -dependent enzymes universally present in all organisms, where they play central roles in regulating numerous biological processes.
Bheda, P., Jing, H., Wolberger, C., Lin, H.   +3 more
openaire   +3 more sources

Substrate specificity of a human-specific esterase

Analytical Biochemistry, 1973
Abstract 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
openaire   +2 more sources

Engineering substrate specificity

Current Opinion in Structural Biology, 1991
Site-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.
Charles Wilson, David A. Agard
openaire   +1 more source