Tetrahydrocolumbamine 2-O-methyltransferase

tetrahydrocolumbamine 2-O-methyltransferase
Identifiers
EC no.2.1.1.89
CAS no.93792-09-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, tetrahydrocolumbamine 2-O-methyltransferase (EC 2.1.1.89) is an enzyme that catalyzes the chemical reaction:[1][2]

(S)-isocorypalmine
+ SAM
 
 
 
 
 
 
 
+ SAH
 

In this methylation reaction, the enzyme uses the cofactor, S-adenosyl methionine (SAM) which transfers a methyl group, giving S-adenosyl-L-homocysteine (SAH) as a by-product. There are several similar transformations in the chemistry of isoquinoline alkaloids.[3][4]

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:5,8,13,13a-tetrahydrocolumbamine 2-O-methyltransferase. This enzyme is also called tetrahydrocolumbamine methyltransferase. This enzyme participates in alkaloid biosynthesis.

References

  1. ^ Enzyme 2.1.1.8 at KEGG Pathway Database.
  2. ^ Beecher CW, Kelleher WJ (1984). "Enzymatic study of the late stages of protoberberine alkaloid biosynthesis". Tetrahedron Lett. 25 (41): 4595–4598. doi:10.1016/S0040-4039(01)91208-0.
  3. ^ Tian, Ya; Kong, Lingzhe; Li, Qi; Wang, Yifan; Wang, Yongmiao; An, Zhoujie; Ma, Yuwei; Tian, Lixia; Duan, Baozhong; Sun, Wei; Gao, Ranran; Chen, Shilin; Xu, Zhichao (2024). "Structural diversity, evolutionary origin, and metabolic engineering of plant specialized benzylisoquinoline alkaloids". Natural Product Reports. 41 (11): 1787–1810. doi:10.1039/d4np00029c. PMID 39360417.
  4. ^ Rueffer M, Zumstein G, Zenk MH (1990). "Partial purification and characterization of S-adenosyl-L-methionine:(S)-tetrahydroprotoberberine cis-N-methyltransferase from suspension-cultured cells of Eschscholtzia and Corydalis" (PDF). Phytochemistry. 29 (12): 3727–3733. doi:10.1016/0031-9422(90)85321-6.