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Information on EC 2.7.1.171 - protein-fructosamine 3-kinase and Organism(s) Mus musculus and UniProt Accession Q9ER35

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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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Mus musculus
UNIPROT: Q9ER35
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The taxonomic range for the selected organisms is: Mus musculus
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
fructosamine-3-kinase
-
fructosamine 3-kinase
-
-
fructose-3-kinase
-
-
ketosamine 3-kinase 1
-
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 + D-fructose
ADP + O3-phosphono-D-fructose
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)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
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 + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
show the reaction diagram
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 + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
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
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
1-deoxy-1-morpholin-4-yl-D-fructose
pH 7.8, 30°C
0.001
N2-(1-deoxy-D-fructosyl)-glycine
pH 7.8, 30°C
0.0074
N6-(1-deoxy-D-fructosyl)-lysine
pH 7.8, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
assay at
7.8
-
asay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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
highest levels of expression in bone marrow, brain, spleen and kidney
Manually annotated by BRENDA team
expressed at low levels
Manually annotated by BRENDA team
highest levels of expression in bone marrow, brain, spleen and kidney
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
Fn3k-/- mice look healthy and have normal blood glucose and serum fructosamine levels. Their level of haemoglobin-bound fructosamines is approx. 2.5-fold higher than that of control (Fn3k+/+) or Fn3k+/- mice. Other intracellular proteins are also significantly more glycated in Fn3k-/- mice in erythrocytes and in brain, kidney, liver and skeletal muscle, indicating that FN3K removes fructosamines from intracellular proteins in vivo
metabolism
despite its ability to reduce the glycation of intracellular islet proteins, fructosamine-3-kinase is neither required for the maintenance of beta-cell survival and function under control conditions nor involved in protection against beta-cell glucotoxicity
physiological function
malfunction
-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FN3K_MOUSE
309
0
35032
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
x * 35000, SDS-PAGE
35032
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pascal, S.M.; Veiga-da-Cunha, M.; Gilon, P.; van Schaftingen, E.; Jonas, J.C.
Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations
Am. J. Physiol. Endocrinol. Metab.
298
E586-596
2009
Mus musculus (Q9ER35), Mus musculus
Manually annotated by BRENDA team
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
Veiga da-Cunha, M.; Jacquemin, P.; Delpierre, G.; Godfraind, C.; Theate, I.; Vertommen, D.; Clotman, F.; Lemaigre, F.; Devuyst, O.; van Schaftingen, E.
Increased protein glycation in fructosamine 3-kinase-deficient mice
Biochem. J.
399
257-264
2006
Mus musculus (Q9ER35)
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
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
Delplanque, J.; Delpierre, G.; Opperdoes, F.R.; van Schaftingen, E.
Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein
J. Biol. Chem.
279
46606-46613
2004
Gallus gallus, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team