2.7.1.171: protein-fructosamine 3-kinase
This is an abbreviated version!
For detailed information about protein-fructosamine 3-kinase, go to the full flat file.
Word Map on EC 2.7.1.171
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2.7.1.171
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deglycation
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erythrocyte
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fructoselysine
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protein-bound
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fn3krp
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non-enzymatic
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fn3k-related
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amadori
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endproducts
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dmf
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maillard
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protein-repairing
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glycemia
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ketoamine
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3-kinase-related
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3-deoxyglucosone
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medicine
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analysis
- 2.7.1.171
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deglycation
- erythrocyte
- fructoselysine
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protein-bound
- fn3krp
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non-enzymatic
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fn3k-related
-
amadori
-
endproducts
- dmf
-
maillard
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protein-repairing
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glycemia
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ketoamine
-
3-kinase-related
- 3-deoxyglucosone
- medicine
- analysis
Reaction
Synonyms
AtFN3K, FL3P, FN3K, fructosamine 3 kinase, fructosamine 3-kinase, fructosamine-3-kinase, fructose-3-kinase, HsFN3K, ketosamine 3-kinase 1
ECTree
2.7.1.171 protein-fructosamine 3-kinaseAdvanced search results
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results (Source Tissue
Source Tissue on EC 2.7.1.171 - protein-fructosamine 3-kinase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
highest levels of expression in bone marrow, brain, spleen and kidney
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fructosamine-3-kinase is a functionally active enzyme in human colon tissue, without significant differences between normal mucosa and cancer. The mean level of fructosamine-3-kinase mRNA is significantly lower in cancer than in the corresponding normal colorectal mucosa. The colorectal tumors located on the left side show lower levels of both enzymatic activity and mRNA fructosamine-3-kinase than tumors located in the right side of colon
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cultured fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state show no changes in fructosamine-3-kinase expression relative to untreated cells. FN3K acts as protein repair enzyme and is expressed constitutively in human cells independently of some of the variables altered in the diabetic state
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highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons
highest levels of expression in bone marrow, brain, spleen and kidney
additional information
highest levels of expression in bone marrow, brain, spleen and kidney
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the human erythrocyte FN3K activity, which is stable with time in a single individual, is highly variable from person to person. This variability, which is linked to single nucleotide polymorphisms that are present in the FN3K gene, affects the glycation level of at least one specific site in haemoglobin
the mean erythrocyte FN3K activity does not differ between normoglycaemic subjects and type 1 diabetic patients, but there is a wide interindividual variability in both groups (from about 1 to 4 mU/g haemoglobin). This variability is stable with time and associated with two single nucleotide polymorphisms in the promoter region and exon 6 of the FN3K gene. There is no significant correlation between FN3K activity and the levels of HbA1c, total glycated haemoglobin and haemoglobin fructoselysine residues, either in the normoglycaemic or diabetic group. The glycation level of Lys144 (in beta-chain of hemoglobin) is about twice as high in normoglycaemic subjects with the lowest FN3K activities as compared to those with the highest FN3K activities
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highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons
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the enzyme is present in all tissues, with the highest level of expression in the kidney
highest levels of expression in bone marrow, brain, spleen and kidney
additional information
enzyme FN3K activity is neither age- nor sex-dependent. The various FN3K SNP rs1056534 genotypes show no significant differences in serum FN3K activity. In diabetics, enzyme activity values are comparable to those of the controls. FN3K activity in erythrocytes is significantly higher
additional information
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enzyme FN3K activity is neither age- nor sex-dependent. The various FN3K SNP rs1056534 genotypes show no significant differences in serum FN3K activity. In diabetics, enzyme activity values are comparable to those of the controls. FN3K activity in erythrocytes is significantly higher
additional information
FN3K is more active in tissues containing proteins with long (half-)lives, such as erythrocytes, lens and brain
additional information
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FN3K is more active in tissues containing proteins with long (half-)lives, such as erythrocytes, lens and brain
additional information
the enzyme is more active in tissues with a long half-life (e.g. brain, erythrocytes and lens), but the expression of the genes for FN3K appears to be constitutive and unaffected by environmental signals
additional information
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the enzyme is more active in tissues with a long half-life (e.g. brain, erythrocytes and lens), but the expression of the genes for FN3K appears to be constitutive and unaffected by environmental signals
additional information
no expression is observed in the intestinal mucosa
