| EC |
2.7.1.172 |
| Accepted name: |
protein-ribulosamine 3-kinase |
| Reaction: |
ATP + [protein]-N6-D-ribulosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine |
| Other name(s): |
Fn3KRP; FN3K-related protein; FN3K-RP; ketosamine 3-kinase 2; fructosamine-3-kinase-related protein; ribulosamine/erythrulosamine 3-kinase; ribulosamine 3-kinase |
| Systematic name: |
ATP:[protein]-N6-D-ribulosyl-L-lysine 3-phosphotransferase |
| Comments: |
This enzyme plays a role in freeing proteins from ribulosamines or psicosamines, which might arise from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by EC 2.7.1.171 (protein-fructosamine 3-kinase), which has, in addition, the unique capacity to phosphorylate fructosamines [1]. The plant enzyme also phosphorylates [protein]-N6-D-erythrulosyl-L-lysine [2]. No activity with [protein]-N6-D-fructosyl-L-lysine [1,2]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Collard, F., Delpierre, G., Stroobant, V., Matthijs, G. and 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 (2003) 2888–2895. [PMID: 14633848] |
| 2. |
Fortpied, J., Gemayel, R., Stroobant, V. and van Schaftingen, E. Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme. Biochem. J. 388 (2005) 795–802. [DOI] [PMID: 15705060] |
| 3. |
Payne, L.S., Brown, P.M., Middleditch, M., Baker, E., Cooper, G.J. and Loomes, K.M. Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5′-[p-(fluorosulfonyl)benzoyl]adenosine. Biochem. J. 416 (2008) 281–288. [DOI] [PMID: 18637789] |
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| [EC 2.7.1.172 created 2011] |
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