Information on EC 2.1.1.300 - pavine N-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Thalictrum flavum

EC NUMBER
COMMENTARY hide
2.1.1.300
-
RECOMMENDED NAME
GeneOntology No.
pavine N-methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + (+/-)-pavine = S-adenosyl-L-homocysteine + N-methylpavine
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(+/-)-pavine N-methyltransferase
The enzyme, isolated from the plant Thalictrum flavum, also methylates (R,S)-stylopine and (S)-scoulerine (11%) with lower activity (14% and 11%, respectively).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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 + (+/-)-pavine
S-adenosyl-L-homocysteine + N-methylpavine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + (R,S)-stylopine
S-adenosyl-L-homocysteine + N-methylstylopine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + (S)-scoulerine
S-adenosyl-L-homocysteine + N-methyl-(S)-scoulerine
show the reaction diagram
-
-
-
-
?
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method, hanging-drop vapour-diffusion method at 16°C, crystallized in space group P2(1). The structure is solved at 2.0 A resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterologously expressed in Escherichia coli
-