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・ 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
・ Glutaminyl-peptide cyclotransferase
・ Glutaminyl-tRNA synthase (glutamine-hydrolysing)
・ Glutamyl aminopeptidase
・ Glutamyl endopeptidase
・ Glutamyl endopeptidase II
・ Glutamyl-tRNA reductase
・ Glutaraldehyde
・ Glutarate-semialdehyde dehydrogenase
・ Glutarate—CoA ligase
・ Glutaredoxin
・ Glutaredoxin 2 (bacterial)


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Glutamine—pyruvate transaminase : ウィキペディア英語版
Glutamine—pyruvate transaminase

In enzymology, a glutamine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction
:L-glutamine + pyruvate \rightleftharpoons 2-oxoglutaramate + L-alanine
Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutarate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:pyruvate aminotransferase. Other names in common use include glutaminase II, L-glutamine transaminase L, and glutamine-oxo-acid transaminase. This enzyme participates in glutamate metabolism. It employs one cofactor, pyridoxal phosphate.
==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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