Information on EC 2.7.1.172 - protein-ribulosamine 3-kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.7.1.172
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RECOMMENDED NAME
GeneOntology No.
protein-ribulosamine 3-kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [protein]-N6-D-ribulosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ATP:[protein]-N6-D-ribulosyl-L-lysine 3-phosphotransferase
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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FN3K-RP can act inside erythrocytes as a deglycating enzyme by converting ketoamines into unstable phosphate esters. Potential physiological substrates are psicosamines, which appear to be formed slowly from fructosamines
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-deoxy-1-morpholin-4-yl-D-psicose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-psicose
show the reaction diagram
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-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-ribulose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-ribulose
show the reaction diagram
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-
-
-
?
ATP + N6-D-erythrulosyl-L-lysine
ADP + N6-(O3-phosphono-D-erythrulosyl)-L-lysine
show the reaction diagram
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
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-
-
-
?
ATP + N6-D-ribulosyl-L-lysine
ADP + N6-(O3-phosphono-D-ribulosyl)-L-lysine
show the reaction diagram
ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
show the reaction diagram
ATP + [lysozyme]-N6-D-psicosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
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in contrast with free psicose-lysine, not all psicosamine residues in the glycated lysozyme substrate would be expected to be accessible to the Fn3KRP active site. In addition, local charge effects may influence the relative affinity for psicosamine residues at different sites in the lysozyme substrate
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-
?
ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
show the reaction diagram
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
show the reaction diagram
-
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
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-
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
show the reaction diagram
-
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
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-
?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxy-1-morpholin-4-yl-D-psicose
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1-deoxy-1-morpholin-4-yl-D-ribulose
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1-deoxy-1-morpholino-D-ribulose
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0.25 mM, 50% inhibition
1-deoxy-1-morpholinopsicose
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competitive inhibitor
5'-p-[(fluorosulfonyl)benzoyl]adenosine
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incubation of 0.7 mg/ml Fn3KRP with 0.5 mM inhibitor results in significant activity loss compared with controls. The inhibitor inactivates Fn3KRP by modification of residues at the nucleotide-binding site
N6-D-psicosyl-L-lysine
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ribuloselysine
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0.1 mM, 50% inhibition
additional information
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neither fructosamines (fructoselysine and deoxymorpholinofructose) nor psicoselysine affect the enzymatic activity at concentrations up to 1 mM. No inhibition is observed with ribulosamines bound to the alpha-amino groups of glycine, valine or leucine, or with D-ribulose or D-erythrulose (all tested at 1 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
1-deoxy-1-morpholin-4-yl-D-psicose
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pH 7.8, 30°C
0.0035
1-deoxy-1-morpholin-4-yl-D-ribulose
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pH 7.8, 30°C
0.025 - 0.279
N6-D-erythrulosyl-L-lysine
0.27
N6-D-psicosyl-L-lysine
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pH 7.8, 30°C
0.119 - 0.135
N6-D-ribulosyl-L-lysine
0.008 - 0.104
[lysozyme]-N6-D-erythrulosyl-L-lysine
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0.42
[lysozyme]-N6-D-psicosyl-L-lysine
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pH 7.8, 30°C
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0.274 - 0.659
[lysozyme]-N6-D-ribulosyl-L-lysine
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58
1-deoxy-1-morpholin-4-yl-D-psicose
Homo sapiens
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pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.0064
1-deoxy-1-morpholin-4-yl-D-ribulose
Homo sapiens
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pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.48
N6-D-psicosyl-L-lysine
Homo sapiens
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pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.174
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pH 7.1, 30°C, substrate: N5-D-ribulosyl-L-lysine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
Manually annotated by BRENDA team
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
Manually annotated by BRENDA team
additional information
no expression is observed in the intestinal mucosa
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
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gel filtration
34412
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x * 34412, calculated from sequence
34440
x * 34440, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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recombinant enzyme, partially purified by chromatography on Blue Sepharose
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
human FN3K-RP is transfected in human embryonic kidney cells and expressed
produced in Escherichia coli as an N-terminal fusion protein with His6 tag