Literature summary for 2.6.1.16 extracted from

Nakaishi, Y.; Bando, M.; Shimizu, H.; Watanabe, K.; Goto, F.; Tsuge, H.; Kondo, K.; Komatsu, M.
Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes (2009), FEBS Lett., 583, 163-167.

Search for more literature for 2.6.1.16

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear D-glucosamine 6-phosphate, hanging drop vapor diffusion method, at 20°C using 12% (v/v) isopropanol, 0.8 M ammonium acetate and 40 mM Tris-HCl at pH 8.5	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-glutamine + D-fructose 6-phosphate	Homo sapiens	-	L-glutamate + D-glucosamine 6-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q06210	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamine + D-fructose 6-phosphate	-	Homo sapiens	L-glutamate + D-glucosamine 6-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
GFAT	-	Homo sapiens
glutamine:fructose-6-phosphate amidotransferase	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	glutamine:fructose-6-phosphate amidotransferase is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)