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Information on EC 2.7.1.172 - protein-ribulosamine 3-kinase
for references in articles please use BRENDA:EC2.7.1.172
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.172 protein-ribulosamine 3-kinase
IUBMB 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 . The plant enzyme also phosphorylates [protein]-N6-D-erythrulosyl-L-lysine . No activity with [protein]-N6-D-fructosyl-L-lysine [1,2].
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.7.1.172
-
deglycation
- erythrocytes
- ribose
-
amadori
- 5-phosphate
- fructoselysine
-
nonenzymatic
-
protein-bound
-
maillard
- erythrose
- haemoglobin
-
decomposing
-
tata-less
-
transglycation
- sphingosine
-
protein-repair
-
caat-less
-
ketoamine
-
endproducts
-
non-physiological
Reaction Schemes
showSynonyms
fn3krp, fn3k-rp, fn3k-related protein, fructosamine-3-kinase-related protein, ribulosamine/erythrulosamine 3-kinase, fructosamine 3-kinase-related protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FN3K-related protein
FN3K-RP
ketosamine 3-kinase 2
ribulosamine/erythrulosamine 3-kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [protein]-N6-D-ribulosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
Substrates: CS-0777
Products: -
Products: -
ir
ATP + 1-deoxy-1-morpholin-4-yl-D-psicose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-psicose
Substrates: -
Products: -
Products: -
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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
Substrates: -
Products: -
Products: -
?
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
Substrates: -
Products: -
Products: -
?
ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
ATP + [lysozyme]-N6-D-psicosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-psicosyl)-L-lysine
Substrates: 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
Products: -
Products: -
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ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
ATP + N6-D-erythrulosyl-L-lysine
ADP + N6-(O3-phosphono-D-erythrulosyl)-L-lysine
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Substrates: -
Products: -
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ATP + N6-D-erythrulosyl-L-lysine
ADP + N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
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ATP + N6-D-ribulosyl-L-lysine
ADP + N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
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ATP + N6-D-ribulosyl-L-lysine
ADP + N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
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ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
?
ATP + [lysozyme]-N6-D-erythrulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-erythrulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
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ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
?
ATP + [lysozyme]-N6-D-ribulosyl-L-lysine
ADP + [lysozyme]-N6-(O3-phosphono-D-ribulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
?
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
Substrates: 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
Products: -
Products: -
?
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
Substrates: 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
Products: -
Products: -
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
Substrates: -
Products: -
Products: -
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme does not act on fructosy-L-lysine or lysozyme glycated with glucose or allose
Products: -
Products: -
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additional information
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Substrates: acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
Products: -
Products: -
?
additional information
?
-
-
Substrates: FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
Products: -
Products: -
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additional information
?
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Substrates: FN3K-RP progressively phosphorylates haemoglobin from erythrocytes that had been incubated with allose or ribose
Products: -
Products: -
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additional information
?
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Substrates: FN3K-RP progressively phosphorylates haemoglobin from erythrocytes that had been incubated with allose or ribose
Products: -
Products: -
?
additional information
?
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Substrates: acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
Products: -
Products: -
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additional information
?
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Substrates: ribuloseglycine, ribulosevaline and ribuloseleucine are phosphorylated at 510% of the rate observed with 1 mM ribuloselysine, whereas no detectable phosphorylation (<1% of the rate observed with ribuloselysine) is observed with fructoselysine, deoxymorpholinofructose, D-ribulose and D-erythrulose. The purified enzyme does not phosphorylate protein-bound fructosamines, psicosamines or ribulosamine 5-phosphates, but does act on protein-bound ribulosamines and erythrulosamines
Products: -
Products: -
?
additional information
?
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Substrates: acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
Products: -
Products: -
?
additional information
?
-
-
Substrates: acts best on free lysine and cadaverine derivatives, but not on ribulosamines bound to the alpha amino group of amino acids. Phosphorylates protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
Substrates: CS-0777
Products: -
Products: -
ir
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
Substrates: 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
Products: -
Products: -
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
Substrates: 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
Products: -
Products: -
?
ATP + [protein]-N6-D-ribulosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-p-[(fluorosulfonyl)benzoyl]adenosine
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
additional information
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Autoimmune Diseases
Enzymatic kinetics regarding reversible metabolism of CS-0777, a sphingosine 1-phosphate receptor modulator, via phosphorylation and dephosphorylation in humans.
Diabetes Complications
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes.
Hyperglycemia
Some clues as to the regulation, expression, function, and distribution of fructosamine-3-kinase and fructosamine-3-kinase-related protein.
Kidney Diseases
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes.
Pulmonary Disease, Chronic Obstructive
FN3K expression in COPD: a potential comorbidity factor for cardiovascular disease.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.06
(R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
pH 7.4, 37°C, recombinant enzyme FN3K-RP
additional information
additional information
Michaelis-Menten kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.58
1-deoxy-1-morpholin-4-yl-D-psicose
Homo sapiens
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.0064
1-deoxy-1-morpholin-4-yl-D-ribulose
Homo sapiens
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
brenda
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
brenda
additional information
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
brenda
activity of fructosamine 3-kinase-related protein is several-fold higher than fructosamine 3-kinase
brenda
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
brenda
highest levels of expression in bone marrow, brain, spleen, kidney, and lens
brenda
additional information
no expression is observed in the intestinal mucosa
brenda
additional information
-
no expression is observed in the intestinal mucosa
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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
physiological function
CS-0777, a candidate compound for autoimmune diseases, becomes phosphorylated to an active metabolite, M1, by fructosamine 3-kinase (FN3K, EC 2.7.1.171) and FN3K-related protein (FN3K-RP), and (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate is reverted back to CS-0777 by alkaline phosphatase (ALP) in the body
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, partially purified by chromatography on Blue Sepharose
recombinant enzyme, partially purified by chromatography on Blue Sepharose
recombinant enzyme, partially purified by chromatography on Blue Sepharose
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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
human FN3K-RP is transfected in human embryonic kidney cells and expressed
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
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produced in Escherichia coli as an N-terminal fusion protein with His6 tag
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Collard, F.; Wiame, E.; Bergans, N.; Fortpied, J.; Vertommen, D.; Vanstapel, F.; Delpierre, G.; van Schaftingen, E.
Fructosamine 3-kinase-related protein and deglycation in human erythrocytes
Biochem. J.
382
137-143
2004
Homo sapiens (Q9HA64), Homo sapiens
brenda
Fortpied, J.; Gemayel, R.; Stroobant, V.; van Schaftingen, E.
Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme
Biochem. J.
388
795-802
2005
Spinacia oleracea, Arabidopsis thaliana
brenda
Payne, L.S.; Brown, P.M.; Middleditch, M.; Baker, E.; Cooper, G.J.; 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
281-288
2008
Homo sapiens (Q9HA64), Homo sapiens
brenda
Collard, F.; Delpierre, G.; Stroobant, V.; Matthijs, G.; 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
2888-2895
2004
Homo sapiens (Q9HA64), Homo sapiens, Mus musculus (Q8K274), Mus musculus
brenda
Gemayel, R.; Fortpied, J.; Rzem, R.; Vertommen, D.; Veiga-da-Cunha, M.; van Schaftingen, E.
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation
FEBS J.
274
4360-4374
2007
Lactiplantibacillus plantarum, Staphylococcus aureus, Thermus thermophilus, Enterococcus faecium
brenda
Delplanque, J.; Delpierre, G.; Opperdoes, F.R.; van Schaftingen, E.
Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein
J. Biol. Chem.
279
46606-46613
2004
Rattus norvegicus
brenda
Inaba, S.I.; Yamaguchi-Goto, M.; Tanaka-Takanaka, K.; Yonesu, K.; Sakurai, H.; Kubota, K.; Izumi, T.
Enzymatic kinetics regarding reversible metabolism of CS-0777, a sphingosine 1-phosphate receptor modulator, via phosphorylation and dephosphorylation in humans
Xenobiotica
48
258-268
2018
Homo sapiens (Q9HA64), Homo sapiens
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.172)
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