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・ Gluconate dehydratase
・ Gluconeogenesis
・ Gluconic acid
・ Glucono delta-lactone
・ Gluconobacter
・ Gluconobacter thailandicus
・ Gluconokinase
・ Gluconolactonase
・ Glucoraphanin
・ Glucosaminate ammonia-lyase
・ Glucosamine
・ Glucosamine kinase
・ Glucosamine N-acetyltransferase
・ Glucosamine-1-phosphate N-acetyltransferase
・ Glucosamine-6-phosphate deaminase
Glucosamine-phosphate N-acetyltransferase
・ Glucosaminephosphate isomerase
・ Glucosaminyl 3-O-sulfotransferase
・ Glucosaminylgalactosylglucosylceramide beta-galactosyltransferase
・ Glucose
・ Glucose 1,6-bisphosphate
・ Glucose 1-dehydrogenase
・ Glucose 1-dehydrogenase (NAD+)
・ Glucose 1-dehydrogenase (NADP+)
・ Glucose 1-phosphate
・ Glucose 6-phosphatase
・ Glucose 6-phosphate
・ Glucose clamp technique
・ Glucose cycle
・ Glucose dehydrogenase (acceptor)


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Glucosamine-phosphate N-acetyltransferase : ウィキペディア英語版
Glucosamine-phosphate N-acetyltransferase

In enzymology, a glucosamine-phosphate N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
:acetyl-CoA + D-glucosamine 6-phosphate \rightleftharpoons CoA + N-acetyl-D-glucosamine 6-phosphate
Thus, the two substrates of this enzyme are acetyl-CoA and D-glucosamine 6-phosphate, whereas its two products are CoA and N-acetyl-D-glucosamine 6-phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase. Other names in common use include phosphoglucosamine transacetylase, phosphoglucosamine acetylase, glucosamine-6-phosphate acetylase, D-glucosamine-6-P N-acetyltransferase, aminodeoxyglucosephosphate acetyltransferase, glucosamine 6-phosphate acetylase, glucosamine 6-phosphate N-acetyltransferase, N-acetylglucosamine-6-phosphate synthase, phosphoglucosamine N-acetylase, glucosamine-phosphate N-acetyltransferase, and glucosamine-6-phosphate N-acetyltransferase. This enzyme participates in glutamate metabolism and aminosugars metabolism.
==Structural studies==

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .

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