Biology:Fructosamine kinase family

From HandWiki
Revision as of 04:02, 11 February 2024 by Wincert (talk | contribs) (fix)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Fructosamin_kin
Identifiers
SymbolFructosamin_kin
PfamPF03881
Pfam clanCL0016
InterProIPR016477

In molecular biology the fructosamine kinase family is a family of enzymes. This family includes eukaryotic fructosamine-3-kinase enzymes which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructoseglycine, fructose and glycated lysozyme.[1] The family also includes ketosamine-3-kinases (KT3K). Ketosamines derive from a non-enzymatic reaction between a sugar and a protein.[2] Ketosamine-3-kinases (KT3K) catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair.[3]

The function of the prokaryotic members of this group has not been established. However, several lines of evidence indicate that they may function as fructosamine-3-kinases (FN3K). First, they are similar to characterised FN3K from mouse and human. Second, the Escherichia coli members are found in close proximity on the genome to fructose-6-phosphate kinase (PfkB). Last, FN3K activity has been found in the blue-green algae Anacystis montana indicating such activity-directly demonstrated in eukaryotes-is nonetheless not confined to eukaryotes.[4]

References

  1. "Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase". Diabetes 49 (10): 1627–34. October 2000. doi:10.2337/diabetes.49.10.1627. PMID 11016445. 
  2. Armbruster DA (December 1987). "Fructosamine: structure, analysis, and clinical usefulness". Clin. Chem. 33 (12): 2153–63. doi:10.1093/clinchem/33.12.2153. PMID 3319287. 
  3. "A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines". Diabetes 52 (12): 2888–95. December 2003. doi:10.2337/diabetes.52.12.2888. PMID 14633848. 
  4. "Distribution of adenosine 5'-triphosphate (ATP)-dependent hexose kinases in microorganisms". BioSystems 10 (3): 265–82. August 1978. doi:10.1016/0303-2647(78)90008-4. PMID 214181. 
This article incorporates text from the public domain Pfam and InterPro: IPR016477