| Entry |
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| Name |
protein-fructosamine 3-kinase;
FN3K;
fructosamine 3-kinase
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| Class |
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with an alcohol group as acceptor
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| Sysname |
ATP:[protein]-N6-D-fructosyl-L-lysine 3-phosphotransferase
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| Reaction(IUBMB) |
ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
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| Substrate |
ATP [CPD: C00002];
[protein]-N6-D-fructosyl-L-lysine
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| Product |
ADP [CPD: C00008];
[protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
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| Comment |
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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| History |
EC 2.7.1.171 created 2011
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| Orthology |
| K15522 | protein-fructosamine 3-kinase |
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| Genes |
» show all
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| Reference |
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| Authors |
Szwergold BS, Howell S, Beisswenger PJ |
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| Title |
Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. |
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| Journal |
Diabetes 50:2139-47 (2001) |
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| Sequence |
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| Reference |
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| Authors |
Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E |
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| Title |
Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.7.1.171 |
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