Information on EC 2.1.1.22 - carnosine N-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.22
-
RECOMMENDED NAME
GeneOntology No.
carnosine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Histidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:carnosine N-methyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37256-93-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
actin peptide H + S-adenosyl-L-methionine
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
show the reaction diagram
-
synthetic peptide based on amino acid sequence of actin
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S-adenosyl-L-methionine + 3-aminobutanoyl-His
S-adenosyl-L-homocysteine + 3-aminobutanoyl-Ntau-methyl-His
show the reaction diagram
-
about 50% of the activity with carnosine
-
?
S-adenosyl-L-methionine + 3-aminobutanoyl-His
S-adenosyl-L-homocysteine + 3-aminobutanoyl-Ntau-methyl-L-His
show the reaction diagram
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
show the reaction diagram
S-adenosyl-L-methionine + Gly-Gly-His
S-adenosyl-L-homocysteine + Gly-Gly-Ntau-methyl-L-His
show the reaction diagram
S-adenosyl-L-methionine + Gly-His
S-adenosyl-L-homocysteine + Gly-Ntau-methyl-L-His
show the reaction diagram
S-adenosyl-L-methionine + homocarnosine
S-adenosyl-L-homocysteine + homoanserine
show the reaction diagram
S-adenosyl-L-methionine + L-histidine
S-adenosyl-L-homocysteine + Ntau-methyl-L-histidine
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
actin peptide H + S-adenosyl-L-methionine
actin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
show the reaction diagram
-
synthetic peptide based on amino acid sequence of actin
-
-
S-adenosyl-L-methionine + carnosine
S-adenosyl-L-homocysteine + anserine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
inhibitory, reversible by addition of EDTA
Mn2+
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inhibitory, reversible by addition of EDTA
Zn2+
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inhibitory, reversible by addition of EDTA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
Actin peptide H
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-
-
1.646 - 6.59
carnosine
0.025 - 0.09
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.008
carnosine
0.011 - 0.078
S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0005
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36375
1 * 36375, calculated, 1 * 38000, gel filtration of recombinant protein
38000
1 * 36375, calculated, 1 * 38000, gel filtration of recombinant protein
45000
gel filtration
85000
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gel filtration, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 36375, calculated, 1 * 38000, gel filtration of recombinant protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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30% loss of activity when heated for 10 min in presence of carnosine, 70% loss of activity within 3 min in absence of carnosine; no loss of activity within 5 min in presence of carnosine
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable on freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, very stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 and HEK-293T cells
expression in COS-7 cell and HeLa cell