Information on EC 2.1.1.22 - carnosine N-methyltransferase:

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The expected taxonomic range for this enzyme is: Amniota


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EC NUMBERCOMMENTARY
2.1.1.22-

RECOMMENDED NAMEGeneOntology No.
carnosine N-methyltransferaseGO:0030735

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
methyl group transfer----

PATHWAYKEGG LinkMetaCyc Link
Histidine metabolism00340 -

SYSTEMATIC NAMEIUBMB Comments
S-adenosyl-L-methionine:carnosine N-methyltransferase-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

CAS REGISTRY NUMBERCOMMENTARY
37256-93-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Cavia porcellus-485238--Manually annotated by BRENDA team
Felis catus-485238--Manually annotated by BRENDA team
Gallus gallus-485238--Manually annotated by BRENDA team
Oryctolagus cuniculus-485238, 485239--Manually annotated by BRENDA team
Rattus norvegicus-485238--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
actin peptide H + S-adenosyl-L-methionineactin peptide H methylated at N1-position of histidine + S-adenosyl-L-homocysteine
show the reaction diagram
Oryctolagus cuniculus-synthetic peptide based on amino acid sequence of actin485239-485239-
S-adenosyl-L-methionine + carnosineS-adenosyl-L-homocysteine + anserine
show the reaction diagram
Gallus gallus, Cavia porcellus, Rattus norvegicus--485238-485238?
S-adenosyl-L-methionine + carnosineS-adenosyl-L-homocysteine + anserine
show the reaction diagram
Oryctolagus cuniculus--485239---
S-adenosyl-L-methionine + carnosineS-adenosyl-L-homocysteine + anserine
show the reaction diagram
Oryctolagus cuniculus, Felis catus--485238-485238?
S-adenosyl-L-methionine + carnosineS-adenosyl-L-homocysteine + anserine
show the reaction diagram
Gallus gallus, Cavia porcellus, Rattus norvegicus, Oryctolagus cuniculus, Felis catus-biosynthesis of anserine485238-485238?
S-adenosyl-L-methionine + histidineS-adenosyl-L-homocysteine + methylhistidine
show the reaction diagram
Cavia porcellus, Oryctolagus cuniculus--485238-485238?
S-adenosyl-L-methionine + histidineS-adenosyl-L-homocysteine + methylhistidine
show the reaction diagram
Oryctolagus cuniculus--485239-485239?
S-adenosyl-L-methionine + homocarnosineS-adenosyl-L-homocysteine + homoanserine
show the reaction diagram
Cavia porcellus, Rattus norvegicus--485238-485238?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
No entries in this field

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Gallus gallus-inhibitory, reversible by addition of EDTA485238
Mn2+Gallus gallus-inhibitory, reversible by addition of EDTA485238
Zn2+Gallus gallus-inhibitory, reversible by addition of EDTA485238

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.5-Actin peptide HOryctolagus cuniculus--485239-
4-carnosineGallus gallus--485238 2D-image
0.09-S-adenosyl-L-methionineGallus gallus--485238 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.0005-Gallus gallus-purified enzyme485238

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.58.5Gallus gallus--485238

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
69Gallus gallus--485238

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainCavia porcellus, Gallus gallus, Rattus norvegicus-low activity485238Manually annotated by BRENDA team
heartCavia porcellus, Rattus norvegicus-low activity485238Manually annotated by BRENDA team
kidneyCavia porcellus, Felis catus-much lower activity than in muscle485238Manually annotated by BRENDA team
kidneyGallus gallus-about the same activity as in muscle; much lower activity than in muscle485238Manually annotated by BRENDA team
kidneyOryctolagus cuniculus-much lower activity than in muscle485238Manually annotated by BRENDA team
kidneyRattus norvegicus--485238Manually annotated by BRENDA team
liverGallus gallus-same activity than in muscle485238Manually annotated by BRENDA team
liverRattus norvegicus-20% of activity in muscle485238Manually annotated by BRENDA team
lungCavia porcellus, Rattus norvegicus--485238Manually annotated by BRENDA team
muscleCavia porcellus, Felis catus, Gallus gallus, Rattus norvegicus--485238Manually annotated by BRENDA team
muscleOryctolagus cuniculus--485238, 485239Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
solubleGallus gallus---485238Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
85000-Oryctolagus cuniculus-gel filtration, sucrose density gradient centrifugation485239

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
50-Gallus gallus-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 carnosine485238

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
stable on freezing and thawingGallus gallus-485238

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20C, very stableGallus gallus-485238

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
partialGallus gallus-485238

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
485238McManus, R.Enzymatic synthesis of anserine in skeletal muscle by N-methylation of carnosineJ. Biol. Chem.2371207-12111962Cavia porcellus, Felis catus, Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus-
485239Raghavan, M.; Lindberg, U.; Schutt, C.The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymesEur. J. Biochem.210311-3181992Oryctolagus cuniculus PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.22)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)