Information on EC 2.1.1.291 - (R,S)-reticuline 7-O-methyltransferase

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The expected taxonomic range for this enzyme is: Papaver somniferum

EC NUMBER
COMMENTARY hide
2.1.1.291
-
RECOMMENDED NAME
GeneOntology No.
(R,S)-reticuline 7-O-methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + (R)-reticuline = S-adenosyl-L-homocysteine + (R)-laudanine
show the reaction diagram
(2)
-
-
-
S-adenosyl-L-methionine + (S)-reticuline = S-adenosyl-L-homocysteine + (S)-laudanine
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
papaverine biosynthesis
-
-
Isoquinoline alkaloid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(R,S)-reticuline 7-O-methyltransferase
The enzyme from the plant Papaver somniferum (opium poppy) methylates (S)- and (R)-reticuline with equal efficiency and is involved in the biosynthesis of tetrahydrobenzylisoquinoline alkaloids.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in in tetrahydrobenzylisoquinoline biosynthesis
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 + (R)-reticuline
S-adenosyl-L-homocysteine + (R)-laudanine
show the reaction diagram
S-adenosyl-L-methionine + (R,S)-orientaline
?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + (S)-reticuline
S-adenosyl-L-homocysteine + (S)-laudanine
show the reaction diagram
S-adenosyl-L-methionine + guaiacol
?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + isovanillic acid
?
show the reaction diagram
-
-
-
?
additional information
?
-
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
S-adenosyl-L-methionine + (R)-reticuline
S-adenosyl-L-homocysteine + (R)-laudanine
show the reaction diagram
Q6WUC2
the enzyme is involved in tetrahydrobenzylisoquinoline biosynthesis
-
-
?
S-adenosyl-L-methionine + (S)-reticuline
S-adenosyl-L-homocysteine + (S)-laudanine
show the reaction diagram
Q6WUC2
the enzyme is involved in tetrahydrobenzylisoquinoline biosynthesis
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
(R)-Reticuline
pH 8.0, 35C
0.016
(S)-reticuline
pH 8.0, 35C
0.017
guaiacol
pH 8.0, 35C
0.014
isovanillic acid
pH 8.0, 35C
0.15 - 0.36
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
(R)-Reticuline
0.1
guaiacol
Papaver somniferum
Q6WUC2
pH 8.0, 35C
0.02
isovanillic acid
Papaver somniferum
Q6WUC2
pH 8.0, 35C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.2
(R)-Reticuline
Papaver somniferum
Q6WUC2
pH 8.0, 35C
5080
4.5
(S)-reticuline
Papaver somniferum
Q6WUC2
pH 8.0, 35C
2631
5.9
guaiacol
Papaver somniferum
Q6WUC2
pH 8.0, 35C
359
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
methylation of (R,S)-isoorientaline
7.5
isovanillic acid
8
methylation of guaiacol, (R)-reticuline and (S)-reticuline
9
methylation of (R)-protosinomenine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
methylation of guaiacol, (R)-reticuline and (S)-reticuline
37 - 41
methylation of (R,S)-isoorientaline and isovanillic acid
39
methylation of (R)-protosinomenine
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is found predominantly in parenchyma cells within the vascular bundle
Manually annotated by BRENDA team
-
the enzyme is found in the pericycle within the stele
Manually annotated by BRENDA team
-
the enzyme is found predominantly in parenchyma cells within the vascular bundle
Manually annotated by BRENDA team
-
the enzyme is found predominantly in parenchyma cells within the vascular bundle
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 39841, calculated from sequence; 2 * 43000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the recombinant protein is then expressed in Spodoptera frugiperda Sf9 cells in a baculovirus expression vector