(RS)-norcoclaurine 6-O-methyltransferase

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In enzymology, a (RS)-norcoclaurine 6-O-methyltransferase (EC 2.1.1.128) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + (RS)-norcoclaurine $\rightleftharpoons$ S-adenosyl-L-homocysteine + (RS)-coclaurine

Thus, the two substrates of this enzyme are S-adenosyl methionine and (R,S)-norcoclaurine, whereas its two products are S-adenosylhomocysteine and (R,S)-coclaurine.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(RS)-norcoclaurine 6-O-methyltransferase. This enzyme participates in alkaloid biosynthesis i.

[edit] References

IUBMB entry for 2.1.1.128
BRENDA references for 2.1.1.128 (Recommended.)
PubMed references for 2.1.1.128
PubMed Central references for 2.1.1.128
Google Scholar references for 2.1.1.128
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Sato F, Tsujita T, Katagiri Y, Yoshida S, Yamada Y (1994). "Purification and characterization of S-adenosyl-L-methionine: norcoclaurine 6-O-methyltransferase from cultured Coptis japonica cells". Eur. J. Biochem. 225: 125–31. doi:10.1111/j.1432-1033.1994.00125.x. PMID 7925429.
Stadler R, Zenk MH (1990). "A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline reticuline". Liebigs Ann. Chem.: 555–562.