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 (fŏs′fər-ə-lās′, -lāz′)
Any of a class of enzymes that catalyze the attachment of a phosphate group to another molecule.


(fɒsˈfɒrɪˌleɪs; -ˌleɪz)
(Biochemistry) any of a group of enzymes that catalyse the hydrolysis of glycogen to glucose-1-phosphate
[C20: from phosphorus + -yl + -ase]


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

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.
References in periodicals archive ?
Other topics include the activities of a-amylases in the presence of polyethylene glycols, color and polysaccharide content in sugarcane and sugarbeet juice, and phosphorylases in the production of oligosaccharides.
A third analysis involves comparison of proteins altered post-translationally after toxicant exposure with specific gene transcript changes in kinases, proteases, phosphorylases, conjugating enzymes, and other enzymes that target specific proteins for modification.
The enzymes that can do this include the glucosyltransferases, such as phosphorylases that elongate amylopectin side chains, and branching enzymes that increase the number of branching points.
Starch phosphorylases were extracted following the methods used for amylase and activity measured as described by Steup and Latzko (1979).
The Seattle researchers found that kinases ferry certain chemical subunits, called phosphate groups, from the energy-rich molecule ATP to dormant phosphorylases.
But it's possible to create new or enhanced functionalities for starch by enzymatically changing its structural properties using glucosyltransferases, such as phosphorylases and branching enzymes.
Fosphenytoin itself has no pharmacological activity but is dephosphorylated in vivo by phosphorylases to the active drug, phenytoin.
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