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]
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Reaction(KEGG) |
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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.
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History |
EC 2.1.1.115 created 1999
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Pathway |
| Isoquinoline alkaloid biosynthesis | | Biosynthesis of secondary metabolites |
|
Orthology |
| (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase |
|
Reference |
1 |
Authors |
Frenzel, T., Zenk, M.H. |
Title |
Purification and characterization of three isoforms of S-adenosyl-L-methionine: (R,S)-tetrahydrobenzyl-isoquinoline N-methyltransferase from Berberis koetineana cell cultures. |
Journal |
Phytochemistry 29 (1990) 3491-3497. |
Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 132084-82-3 |
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