| EC |
2.7.1.171 |
| Accepted name: |
protein-fructosamine 3-kinase |
| Reaction: |
ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine |
| Other name(s): |
FN3K; fructosamine 3-kinase |
| Systematic name: |
ATP:[protein]-N6-D-fructosyl-L-lysine 3-phosphotransferase |
| 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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Szwergold, B.S., Howell, S. and Beisswenger, P.J. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes 50 (2001) 2139–2147. [PMID: 11522682] |
| 2. |
Delpierre, G., Rider, M.H., Collard, F., Stroobant, V., Vanstapel, F., Santos, H. and Van Schaftingen, E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes 49 (2000) 1627–1634. [PMID: 11016445] |
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| [EC 2.7.1.171 created 2011] |
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