Information on EC 2.1.1.118 - columbamine O-methyltransferase

for references in articles please use BRENDA:EC2.1.1.118
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.118
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RECOMMENDED NAME
GeneOntology No.
columbamine O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + columbamine = S-adenosyl-L-homocysteine + palmatine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
palmatine biosynthesis
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Isoquinoline alkaloid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:columbamine O-methyltransferase
The product of this reaction is a protoberberine alkaloid that is widely distributed in the plant kingdom. This enzyme is distinct in specificity from EC 2.1.1.88, 8-hydroxyquercetin 8-O-methyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
105843-76-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Berberis aggregata
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Manually annotated by BRENDA team
var. subcaulialate
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + columbamine
S-adenosyl-L-homocysteine + palmatine
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
Columbamine
0.0015
S-adenosyl-L-methionine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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