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Information on EC 2.6.1.16 - glutamine-fructose-6-phosphate transaminase (isomerizing) and Organism(s) Homo sapiens

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IUBMB Comments
Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
gfpt1, gfat1, glms ribozyme, glucosamine-6-phosphate synthase, glutamine:fructose-6-phosphate amidotransferase, glcn-6-p synthase, gfat2, glutamine fructose-6-phosphate amidotransferase, g-6-p synthase, glucosamine 6-phosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-2-deoxy-D-glucose-6-phosphate ketol-isomerase
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-
-
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GFPT1
GlcN-6-P synthase
-
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glucosamine 6-phosphate synthase
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-
-
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glucosamine 6-phosphate synthetase
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-
-
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glucosamine phosphate isomerase (glutamine-forming)
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-
-
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glucosamine synthase
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-
-
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glucosamine-6-phosphate isomerase (glutamine-forming)
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-
-
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glucosamine-6-phosphate synthase
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glucosamine-6-phosphate synthetase
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-
-
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glucosamine:fructose-6-phosphate aminotransferase
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-
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glutamine-fructose 6-phosphate amidotransferase
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-
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glutamine-fructose 6-phosphate aminotransferase
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-
-
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glutamine-fructose-6-phosphate transaminase 1
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glutamine: fructose-6-phosphate amidotransferase 1
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glutamine:fructose-6-phosphate amidotransferase
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glutamine:fructose-6-phosphate aminotransferase
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hexosephosphate aminotransferase
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-
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isomerase, glucosamine phosphate (glutamine-forming)
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L-glutamine fructose 6-phosphate transamidase
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L-glutamine: L-fructose-6-phosphate amidotransferase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
CAS REGISTRY NUMBER
COMMENTARY hide
9030-45-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-gamma-glutamyl-p-nitroanilide + H2O
L-glutamine + p-nitroaniline
show the reaction diagram
-
determination of amidohydrolysing activity
-
-
?
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamine + D-fructose 6-phosphate
L-glutamate + D-glucosamine 6-phosphate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-2-deoxy-D-glucitol-6-phosphate
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inhibitor of the sugar isomerising domain
2-amino-2-deoxy-D-mannitol-6-phosphate
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exhibits stronger affinity for the sugar-binding site of GlcN-6-P synthase than 2-amino-2-deoxy-D-glucitol-6-phosphate
6-diazo-5-oxo-L-norleucine
-
inhibitor of the glutamine binding site
anticapsin
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inhibitor of the glutamine binding site
arabinose oxime 5-phosphate
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inhibitor of the sugar isomerising domain
N3-(4-Methoxyfumaroyl)-L-2,3-diaminopropanoic acid
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acts as active-site-directed inactivator blocking the N-terminal, glutamine-binding domain of the enzyme; inhibitor of the glutamine binding site
N3-bromoacetyl-L-2,3-diaminopropanoic acid
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inhibitor of the glutamine binding site
N3-L-trans-epoxysuccinamoyl-L-2,3-diaminopropanoic acid
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inhibitor of the glutamine binding site
UDP-N-acetylglucosamine
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feed-back inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52 - 1.04
D-fructose 6-phosphate
1.8
L-gamma-glutamyl-p-nitroanilide
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both wild-type and mutant S243E, 37°C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34.8
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GFPT2_HUMAN
682
0
76931
Swiss-Prot
other Location (Reliability: 5)
GFPT1_HUMAN
699
0
78806
Swiss-Prot
other Location (Reliability: 5)
A0A6I8PTT9_HUMAN
625
0
70432
TrEMBL
other Location (Reliability: 5)
B4DN38_HUMAN
607
0
68116
TrEMBL
other Location (Reliability: 1)
B3KMR8_HUMAN
682
0
76906
TrEMBL
other Location (Reliability: 5)
B2RB90_HUMAN
682
0
76959
TrEMBL
other Location (Reliability: 5)
A0A0S2Z4W6_HUMAN
628
0
70933
TrEMBL
other Location (Reliability: 5)
A0A0S2Z4X9_HUMAN
682
0
76931
TrEMBL
other Location (Reliability: 5)
A0A6I8PRN4_HUMAN
609
0
68542
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77000
-
? * 77000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
? * 77000, SDS-PAGE
additional information
-
The fact that the 77 kDa protein expressed in Escherichia coli is sensitive to inhibition by UDP-N-acetylglucosamine is consistent with the idea that mammalian GFAT is comprised of four identical subunits
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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enzyme is phosphorylated in vivo, phosphorylation site is residue S243. Phosphorylation at Ser243 stimulates glucosamine 6-phosphate synthesizing activity, lowers amidohydrolyzing activity in the absence of fructose 6-phosphate, and lowers Km of fructose 6-phosphate 2fold, but has no effect on UDP-GlcNAc inhibition. Phosphorylation is mediated by AMP-activated protein kinase and calcium/calmodulin-dependent kinase II in vitro
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S243E
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increase in activity, 2fold lower Km value for D-fructose 6-phosphate than wild-type
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
isopropanol, 1%, stabilizes during purification
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-25°C, 1 month, 15% activity loss, ammonium sulfate precipitated enzyme
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-80°C, 50 mM Tris-HCl, pH 7.8, 200 mM NaCl, 1 mM fructose 6-phosphate, 2 mM tris(2-carboxyethyl)phosphine hydrochloride, 200 mM imidazole, 10% glycerol, stable for up to 12 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expression in insect cell and Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McKnight, G.L.; Mudri, S.L.; Mathewes, S.L.; Traxinger, R.R.; Marshall, S.; Sheppard, P.O.; O'Hara, P.J.
Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase
J. Biol. Chem.
267
25208-25212
1992
Homo sapiens
Manually annotated by BRENDA team
Kikuchi, H.; Tsuiki, S.
Glucosaminephosphate synthase of human liver
Biochim. Biophys. Acta
422
241-246
1976
Homo sapiens
Manually annotated by BRENDA team
Wojciechowski, M.; Milewski, S.; Mazerski, J.; Borowski, E.
Glucosamine-6-phosphate synthase, a novel target for antifungal agents. Molecular modelling studies in drug design
Acta Biochim. Pol.
52
647-653
2005
Homo sapiens
Manually annotated by BRENDA team
Kunika, K.; Tanahashi, T.; Kudo, E.; Mizusawa, N.; Ichiishi, E.; Nakamura, N.; Yoshikawa, T.; Yamaoka, T.; Yasumo, H.; Tsugawa, K.; Moritani, M.; Inoue, H.; Itakura, M.
Effect of +36T>C in intron 1 on the glutamine: fructose-6-phosphate amidotransferase 1 gene and its contribution to type 2 diabetes in different populations
J. Hum. Genet.
51
1100-1109
2006
Homo sapiens
Manually annotated by BRENDA team
Li, Y.; Roux, C.; Lazereg, S.; LeCaer, J.P.; Laprevote, O.; Badet, B.; Badet-Denisot, M.A.
Identification of a novel serine phosphorylation site in human glutamine:fructose-6-phosphate amidotransferase isoform 1
Biochemistry
46
13163-13169
2007
Homo sapiens
Manually annotated by BRENDA team
Srinivasan, V.; Sandhya, N.; Sampathkumar, R.; Farooq, S.; Mohan, V.; Balasubramanyam, M.
Glutamine fructose-6-phosphate amidotransferase (GFAT) gene expression and activity in patients with type 2 diabetes: inter-relationships with hyperglycaemia and oxidative stress
Clin. Biochem.
40
952-957
2007
Homo sapiens
Manually annotated by BRENDA team
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
FEBS Lett.
583
163-167
2009
Homo sapiens (Q06210), Homo sapiens
Manually annotated by BRENDA team
Chen, Q.; Mueller, J.S.; Pang, P.C.; Laval, S.H.; Haslam, S.M.; Lochmueller, H.; Dell, A.
Global N-linked glycosylation is not significantly impaired in myoblasts in congenital myasthenic syndromes caused by defective glutamine-fructose-6-phosphate transaminase 1 (GFPT1)
Biomolecules
5
2758-2781
2015
Homo sapiens (Q06210), Homo sapiens
Manually annotated by BRENDA team