phosphorylase


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phos·pho·ryl·ase

 (fŏs′fər-ə-lās′, -lāz′)
n.
Any of a class of enzymes that catalyze the attachment of a phosphate group to another molecule.
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.

phosphorylase

(fɒsˈfɒrɪˌleɪs; -ˌleɪz)
n
(Biochemistry) any of a group of enzymes that catalyse the hydrolysis of glycogen to glucose-1-phosphate
[C20: from phosphorus + -yl + -ase]
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014

phos•pho•ryl•ase

(ˈfɒs fər əˌleɪs, -ˌleɪz, fɒsˈfɔr ə-, -ˈfɒr-)

n.
any enzyme, occurring widely in animal and plant tissue, that in the presence of an inorganic phosphate catalyzes the conversion of glycogen into sugar phosphate.
[1935–40]
Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved.
References in periodicals archive ?
The blood concentration of FTD is maintained via TPI, which is an inhibitor of the FTD-degrading enzyme, thymidine phosphorylase.
Lonsurf consists of a thymidine-based nucleoside analog, trifluridine, and the thymidine phosphorylase inhibitor, tipiracil, which increases trifluridine exposure by inhibiting its metabolism by TP.
The decreased expression mechanism of PKC is not fully understood, but many previous in vivo and in vitro studies have shown a strong indication of decreased expression of PKC caused by curcumin acting as a noncompetitive and selective inhibitor of phosphorylase kinase.
The LRMWM contains the following proteins used as markers: phosphorylase b (97 kDa), bovine serum albumin (66 kDa), ovalbumin (45 kDa), carbonic anhydrase (29 kDa), trypsinogen (24 kDa) and tripsic soybean inhibitor (20 kDa).
According to the company, LONSURF consists of a thymidine-based nucleoside analog, trifluridine, and the thymidine phosphorylase (TP) inhibitor, tipiracil, which increases trifluridine exposure by inhibiting its metabolism by TP.
The cells were treated with Z-IETD-FMK (40 [micro]M), Nec1 (50 [micro]M), or Z-IETD-FMK (40 [micro]M) and Nec-1 (50 [micro]M) for 1 h, after which they were treated with TNF-[alpha] (20 ng/mL) for an additional 12 or 24 h, and protein lysates were extracted in radioimmunoprecipitation (RIPA) lysis buffer containing 4% protease inhibitor, 4% phosphorylase inhibitor, and 1% PMSF.
Abnormal cells increase oxidative stress within the cell by catabolizing the thymidine to thymine and 2-deoxy-D-ribose-1-phosphate (that quickly bind with proteins to form glycated proteins) by thymidine phosphorylase (Brown et al., 2000; Brown and Bicknell, 2001).
Methylthioadenosine phosphorylase (MTAP, Table 2, spot 6 and Table 3, spot 2) catalyzes the reversible phosphorolytic cleavage of methylthioadenosine, a by-product of the polyamine biosynthesis, producing methylthioribose-1-phosphate (MTRP) and adenine.
It has been demonstrated that the [alpha]-actinin-3 absence induces metabolic changes towards oxidative metabolism, resulting in higher activity of oxidative enzymes (e.g., citrate synthase) and lower activity of glycolytic enzymes (e.g., lactate dehydrogenase and glycogen phosphorylase) (28).