| Entry |
|
| Name |
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase;
norreticuline N-methyltransferase |
| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
 |
| Sysname |
S-adenosyl-L-methionine:(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline
N-methyltransferase |
| Reaction(IUBMB) |
S-adenosyl-L-methionine +
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline =
S-adenosyl-L-homocysteine +
N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline [RN:R04713] |
| Reaction(KEGG) |
R04713;
(other) R04692 R05211 R05216
 |
| Substrate |
S-adenosyl-L-methionine [CPD:C00019];
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline [CPD:C05201] |
| Product |
S-adenosyl-L-homocysteine [CPD:C00021];
N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline [CPD:C05314] |
| Comment |
Broad substrate specificity for
(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines; including coclaurine,
norcoclaurine, isococlaurine, norarmepavine, norreticuline and
tetrahydropapaverine. Both R- and S-enantiomers are methylated. The
enzyme participates in the pathway leading to benzylisoquinoline
alkaloid synthesis in plants. The physiological substrate is likely
to be coclaurine. The enzyme was earlier termed norreticuline
N-methyltransferase. However, norreticuline has not been found to
occur in nature and that name does not reflect the broad specificity
of the enzyme for (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinolines. |
| Pathway |
PATH: ec00950 Isoquinoline alkaloid biosynthesis |
| Orthology |
KO: K13388 coclaurine N-methyltransferase |
Reference Authors Title
Journal
|
1
Frenzel, T., Zenk, M.H.
Purification and characterization of three isoforms of
S-adenosyl-L-methionine: (R,S)-tetrahydrobenzyl-isoquinoline
N-methyltransferase from Berberis koetineana cell cultures.
Phytochemistry 29 (1990) 3491-3497. |
| Other DBs |
ExplorEnz - The Enzyme Database: 2.1.1.115
IUBMB Enzyme Nomenclature: 2.1.1.115
ExPASy - ENZYME nomenclature database: 2.1.1.115
BRENDA, the Enzyme Database: 2.1.1.115
CAS: 132084-82-3 |
|