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Information on EC 2.7.1.171 - protein-fructosamine 3-kinase and Organism(s) Homo sapiens and UniProt Accession Q9HA64

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IUBMB Comments
Non-enzymic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as [protein]-N6-D-fructosyl-L-lysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from non-enzymically glycated proteins. The phosphorylation destablilizes the [protein]-N6-D-fructosyl-L-lysine adduct and leads to its spontaneous decomposition. cf. EC 2.7.1.172, protein-ribulosamine 3-kinase.
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Homo sapiens
UNIPROT: Q9HA64
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fructosamine-3-kinase, fructosamine 3-kinase, fructosamine 3 kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ketosamine 3-kinase 1
-
fructosamine 3 kinase
-
fructosamine 3-kinase
-
fructosamine-3-kinase
fructose-3-kinase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
show the reaction diagram
phosphorylation destablilizes the fructoselysine adduct and leads to its spontaneous decomposition
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[protein]-N6-D-fructosyl-L-lysine 3-phosphotransferase
Non-enzymic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as [protein]-N6-D-fructosyl-L-lysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from non-enzymically glycated proteins. The phosphorylation destablilizes the [protein]-N6-D-fructosyl-L-lysine adduct and leads to its spontaneous decomposition. cf. EC 2.7.1.172, protein-ribulosamine 3-kinase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
show the reaction diagram
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-psicose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-psicose
show the reaction diagram
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-ribulose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-ribulose
show the reaction diagram
-
-
-
?
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
-
-
-
?
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
show the reaction diagram
CS-0777
-
-
ir
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
show the reaction diagram
ATP + D-fructose
ADP + O3-phosphono-D-fructose
show the reaction diagram
ATP + N-alpha-hippuryl-N-epsilon-psicosyllysine
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
show the reaction diagram
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycylglycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycylglycine
show the reaction diagram
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-L-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-L-valine
show the reaction diagram
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
show the reaction diagram
-
-
-
?
ATP + N5-D-fructosyl-L-ornithine
ADP + N5-(O3-phosphono-D-fructosyl)-L-ornithine
show the reaction diagram
-
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-L-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
show the reaction diagram
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + N6-D-fructosyl-L-lysine
ADP + N6-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
-
-
-
-
?
ATP + Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine
ADP + Nalpha-hippuryl-Nepsilon-(1-deoxy-3-phospho-D-fructosyl)lysine
show the reaction diagram
-
-
Nalpha-hippuryl-Nepsilon-(3-phosphofructosyl)lysine like other 3-phosphofructosylamines, is not stable. Terminating the enzyme reaction with trichloracetic acid stabilises the analyte
-
?
ATP + [hemoglobin]-N6-D-fructosyl-L-lysine
ADP + [hemoglobin]-N6-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
-
mass-spectrometric identification of the fructosamine residues that are removed from hemoglobin in intact erythrocytes as a result of the action of fructosamine-3-kinase: Lys16, Lys61 and Lys139 in the alpha-chain of hemoglobin, Val1, Lys17, Lys59, Lys66, Lys132, and Lys144 in the beta-chain of hemoglobin. Some (e.g. Lys139 in the alph-chain of hemoglobin) are readily phosphorylated to a maximal extent by fructosamine-3-kinase in vitro whereas others (e.g. Val1 in the beta-chain of hemoglobin) are slowly and only very partially phosphorylated
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
show the reaction diagram
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
glycated bovine serum albumin + ATP
?
show the reaction diagram
derived from dialyzed glycated bovine serum albumin
-
-
?
additional information
?
-
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
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
show the reaction diagram
CS-0777
-
-
ir
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
show the reaction diagram
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxy-1-morpholin-4-yl-D-fructose
-
1-deoxy-1-morpholin-4-yl-D-psicose
-
1-deoxy-1-morpholin-4-yl-D-ribulose
-
N6-D-psicosyl-L-lysine
-
1-deoxy-1-morpholinofructose
deoxymorpholinofructose
a competitive inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
1-deoxy-1-morpholin-4-yl-D-fructose
pH 7.8, 30°C
0.16
1-deoxy-1-morpholin-4-yl-D-psicose
pH 7.8, 30°C
0.0026
1-deoxy-1-morpholin-4-yl-D-ribulose
pH 7.8, 30°C
0.14
N6-D-psicosyl-L-lysine
pH 7.8, 30°C
0.922
(R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
pH 7.4, 37°C, recombinant enzyme FN3K
-
0.001 - 0.1
1-deoxy-1-morpholin-4-yl-D-fructose
50
D-fructose
-
pH 8.0, 37°C
0.001 - 0.0022
N2-(1-deoxy-D-fructosyl)-glycine
1.5
N2-(1-deoxy-D-fructosyl)-glycylglycine
-
0.8
N2-(1-deoxy-D-fructosyl)-L-valine
-
0.5
N5-D-fructosyl-L-ornithine
-
pH 8.0, 37°C
0.0072
N6-(1-deoxy-D-fructosyl)-L-lysine
-
0.0072 - 0.0132
N6-(1-deoxy-D-fructosyl)-lysine
0.75
N6-D-fructosyl-L-lysine
-
pH 8.0, 37°C
0.01
[protein]-N6-D-fructosyl-L-lysine
-
pH 8.0, 37°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067
1-deoxy-1-morpholin-4-yl-D-fructose
Homo sapiens
pH 7.8, 30°C
0.69
1-deoxy-1-morpholin-4-yl-D-psicose
Homo sapiens
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.0036
1-deoxy-1-morpholin-4-yl-D-ribulose
Homo sapiens
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.72
N6-D-psicosyl-L-lysine
Homo sapiens
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.08
-
pH 8.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
fructosamine-3-kinase is a functionally active enzyme in human colon tissue, without significant differences between normal mucosa and cancer. The mean level of fructosamine-3-kinase mRNA is significantly lower in cancer than in the corresponding normal colorectal mucosa. The colorectal tumors located on the left side show lower levels of both enzymatic activity and mRNA fructosamine-3-kinase than tumors located in the right side of colon
Manually annotated by BRENDA team
overexpression
Manually annotated by BRENDA team
-
cultured fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state show no changes in fructosamine-3-kinase expression relative to untreated cells. FN3K acts as protein repair enzyme and is expressed constitutively in human cells independently of some of the variables altered in the diabetic state
Manually annotated by BRENDA team
-
highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
starvation and diabetes do not change the level of expression of FN3K in different tissues, and no regulation of FN3K expression is observed in human fibroblasts treated with condition mimicking the diabetic state
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KT3K_HUMAN
309
0
34412
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
35032
x * 35032, calculated from sequence
35171
x * 35171, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
FN3K adopts a protein kinase fold. Structure-function analysis and comparisons, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, partially purified by chromatography on Blue Sepharose
recombinant N-terminally His6-tagged enzyme from Pichia pastoris by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
human FN3K-RP is transfected in human embryonic kidney cells and expressed
expression in Escherichia coli
gene FN3K, constitutive expression, recombinant expression of N-terminally His6-tagged enzyme from the codon-optimized gene in Pichia pastoris under control of the methanol inducible aldehyde oxidase 1 (AOX1) promoter
gene FN3K, DNA and amino acid sequence analysis, genotyping
gene FN3K, located on chromosome 17q25, genotyping
gene FN3K, located on chromosome 17q25.3, genotyping
genotyping of FN3K SNP rs1056534 and the ferroportin SNP rs1156350. FN3K activity depends on the ferroportin Q248H genotypes, with the highest value for the wild-type genotype
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons. Cultured fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state show no changes in fructosamine-3-kinase expression relative to untreated cells. FN3K acts as protein repair enzyme and is expressed constitutively in human cells independently of some of the variables altered in the diabetic state
-
no regulation of the expression of fructose-3-kinase is observed in human fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state
-
the down-regulation of FN3K gene expression in cancer tissue compared with normal mucosa is a characteristic only of the left-sided tumours of the colon
-
the expression of the genes for FN3K appears to be constitutive and unaffected by environmental signals
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
convenient assay for the determination of FN3K activity in erythrocytes, which can be performed in routine laboratories
medicine
FN3K may be a potential predictor of the risk of diabetes complications. Pharmacological modifications of its activity may provide an approach to their prevention
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
van Schaftingen, E.; Collard, F.; Wiame, E.; Veiga-da-Cunha, M.
Enzymatic repair of Amadori products
Amino Acids
42
1143-1150
2012
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Krause, R.; Oehme, A.; Wolf, K.; Henle, T.
A convenient HPLC assay for the determination of fructosamine-3-kinase activity in erythrocytes
Anal. Bioanal. Chem.
386
2019-2025
2006
Homo sapiens
Manually annotated by BRENDA team
Conner, J.R.; Beisswenger, P.J.; Szwergold, B.S.
The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinase-related protein appears to be constitutive and unaffected by environmental signals
Biochem. Biophys. Res. Commun.
323
932-936
2004
Homo sapiens
Manually annotated by BRENDA team
Delpierre, G.; Collard, F.; Fortpied, J.; van Schaftingen, E.
Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes
Biochem. J.
365
801-808
2002
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Delpierre, G.; Veiga-da-Cunha, M.; Vertommen, D.; Buysschaert, M.;, Van Schaftingen E.
Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites
Diabetes Metab.
32
31-39
2005
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Delpierre, G.; Rider, M.H.; Collard, F.; Stroobant, V.; Vanstapel, F.; Santos, H.; van Schaftingen, E.
Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase
Diabetes
49
1627-1634
2000
Mus musculus (Q9ER35), Mus musculus, Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Szwergold, B.S.; Howell, S.; Beisswenger, P.J.
Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo
Diabetes
50
2139-2147
2001
Homo sapiens
Manually annotated by BRENDA team
Collard, F.; Delpierre, G.; Stroobant, V.; Matthijs, G.; van Schaftingen, E.
A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines
Diabetes
52
2888-2895
2004
Mus musculus (Q8K274), Mus musculus, Homo sapiens (Q9HA64), Homo sapiens
Manually annotated by BRENDA team
Mohas, M.; Kisfali, P.; Baricza, E.; Merei, A.; Maasz, A.; Cseh, J.; Mikolas, E.; Szijarto, I.A.; Melegh, B.; Wittmann, I.
A polymorphism within the fructosamine-3-kinase gene is associated with HbA1c levels and the onset of type 2 diabetes mellitus
Exp. Clin. Endocrinol. Diabetes
118
209-212
2009
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Notarnicola, M.; Caruso, M.G.; Tutino, V.; Guerra, V.; Frisullo, S.; Altomare, D.F.; Misciagna, G.
Reduced fructosamine-3-kinase activity and its mRNA in human distal colorectal carcinoma
Genes Nutr.
5
257-262
2010
Homo sapiens
Manually annotated by BRENDA team
Delpierrre, G.; Vertommen. D.; Communi, D.; Rider, M.H.; van Schaftingen, E.
Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin
J. Biol. Chem.
279
27613-27620
2004
Homo sapiens
Manually annotated by BRENDA team
Caruso, M.G.; Notarnicola, M.; Altomare, D.F.; Misciagna, G.
Gene expression of fructosamine 3 kinase in patients with colorectal cancer
Oncology
73
72-75
2008
Homo sapiens
Manually annotated by BRENDA team
Hellwig, A.; Scherber, A.; Koehler, C.; Hanefeld, M.; Henle, T.
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes
Clin. Chem. Lab. Med.
52
93-101
2014
Homo sapiens (Q9H479)
-
Manually annotated by BRENDA team
Avemaria, F.; Carrera, P.; Lapolla, A.; Sartore, G.; Chilelli, N.C.; Paleari, R.; Ambrosi, A.; Ferrari, M.; Mosca, A.
Possible role of fructosamine 3-kinase genotyping for the management of diabetic patients
Clin. Chem. Lab. Med.
53
1315-1320
2015
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Cikomola, J.C.; Kishabongo, A.S.; Vandepoele, K.; Mulder, M.; Katchunga, P.B.; Laukens, B.; Schie, L.V.; Grootaert, H.; Callewaert, N.; Speeckaert, M.M.; Delanghe, J.R.
A simple colorimetric assay for measuring fructosamine 3 kinase activity
Clin. Chem. Lab. Med.
55
154-159
2017
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Skrha, J.; Muravska, A.; Flekac, M.; Horova, E.; Novak, J.; Novotny, A.; Prazny, M.; Skrha, J.; Kvasnicka, J.; Landova, L.; Jachymova, M.; Zima, T.; Kalousova, M.
Fructosamine 3-kinase and glyoxalase I polymorphisms and their association with soluble RAGE and adhesion molecules in diabetes
Physiol. Res.
63 Suppl 2
S283-S291
2014
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Sartore, G.; Ragazzi, E.; Burlina, S.; Paleari, R.; Chilelli, N.C.; Mosca, A.; Avemaria, F.; Lapolla, A.
Role of fructosamine-3-kinase in protecting against the onset of microvascular and macrovascular complications in patients with T2DM
BMJ Open Diabetes Res. Care
8
e001256
2020
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Sanghvi, V.R.; Leibold, J.; Mina, M.; Mohan, P.; Berishaj, M.; Li, Z.; Miele, M.M.; Lailler, N.; Zhao, C.; de Stanchina, E.; Viale, A.; Akkari, L.; Lowe, S.W.; Ciriello, G.; Hendrickson, R.C.; Wendel, H.G.
The oncogenic action of NRF2 depends on de-glycation by fructosamine-3-kinase
Cell
178
807-819.e21
2019
Homo sapiens (Q9H479)
Manually annotated by BRENDA team
Dunmore, S.J.; Al-Derawi, A.S.; Nayak, A.U.; Narshi, A.; Nevill, A.M.; Hellwig, A.; Majebi, A.; Kirkham, P.; Brown, J.E.; Singh, B.M.
Evidence that differences in fructosamine-3-kinase activity may be associated with the glycation gap in human diabetes
Diabetes
67
131-136
2018
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
De Bruyne, S.; Van Dorpe, J.; Himpe, J.; Van Biesen, W.; Delanghe, S.; Speeckaert, M.M.; Delanghe, J.R.
Detection and characterization of a biochemical signature associated with diabetic nephropathy using near-infrared spectroscopy on tissue sections
J. Clin. Med.
8
2869
2019
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team
Shrestha, S.; Katiyar, S.; Sanz-Rodriguez, C.E.; Kemppinen, N.R.; Kim, H.W.; Kadirvelraj, R.; Panagos, C.; Keyhaninejad, N.; Colonna, M.; Chopra, P.; Byrne, D.P.; Boons, G.J.; van der Knaap, E.; Eyers, P.A.; Edison, A.S.; Wood, Z.A.; Kannan, N.
A redox-active switch in fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily
Sci. Signal.
13
eaax6313
2020
Arabidopsis thaliana, Homo sapiens (Q9H479)
Manually annotated by BRENDA team
Inaba, S.I.; Yamaguchi-Goto, M.; Tanaka-Takanaka, K.; Yonesu, K.; Sakurai, H.; Kubota, K.; Izumi, T.
Enzymatic kinetics regarding reversible metabolism of CS-0777, a sphingosine 1-phosphate receptor modulator, via phosphorylation and dephosphorylation in humans
Xenobiotica
48
258-268
2018
Homo sapiens (Q9H479), Homo sapiens
Manually annotated by BRENDA team