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・ Glutamate-1-semialdehyde 2,1-aminomutase
・ Glutamate-5-semialdehyde
・ Glutamate-5-semialdehyde dehydrogenase
・ Glutamate-glutamine cycle
・ Glutamatergic
・ Glutamate–cysteine ligase
・ Glutamate—ethylamine ligase
・ Glutamate—methylamine ligase
・ Glutamate—prephenate aminotransferase
・ Glutamate—putrescine ligase
・ Glutamate—tRNA ligase
・ Glutamate—tRNA(Gln) ligase
・ Glutamic acid
・ Glutamic acid (data page)
・ Glutamic protease
Glutamin-(asparagin-)ase
・ Glutaminase
・ Glutamine
・ Glutamine (data page)
・ Glutamine amidotransferase
・ Glutamine N-acyltransferase
・ Glutamine N-phenylacetyltransferase
・ Glutamine oxoglutarate aminotransferase
・ Glutamine synthetase
・ Glutamine—fructose-6-phosphate transaminase (isomerizing)
・ Glutamine—phenylpyruvate transaminase
・ Glutamine—pyruvate transaminase
・ Glutamine—scyllo-inositol transaminase
・ Glutamine—tRNA ligase
・ Glutaminolysis


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Glutamin-(asparagin-)ase : ウィキペディア英語版
Glutamin-(asparagin-)ase

In enzymology, a glutamin-(asparagin-)ase () is an enzyme that catalyzes the chemical reaction
:L-glutamine + H2O \rightleftharpoons L-glutamate + NH3
Thus, the two substrates of this enzyme are L-glutamine and H2O, whereas its two products are L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-glutamine(L-asparagine) amidohydrolase. This enzyme participates in 4 metabolic pathways: glutamate metabolism, alanine and aspartate metabolism, d-glutamine and d-glutamate metabolism, and nitrogen metabolism.
==Structural studies==

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .

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