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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 35, Number 1
BKCSDE 35(1)
January 20, 2014 

Molecular Modeling and Docking Studies of 3'-Hydroxy-N-methylcoclaurine 4'-O-Methyltransferase from Coptis chinensis
Qiankun Zhu, Mengli Zhu, Gaotao Fan, Jiaxin Zou, Peichun Feng, Zubi Liu, Wanjun Wang*
3'-Hydroxy-N-methylcoclaurine 4'-O-methyltransferase, Molecular modeling, Molecular docking, Coptis chinensis
Coptis chinensis 3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase (HOMT), an essential enzyme in the berberine biosynthetic pathway, catalyzes the methylation of 3'-hydroxy-N-methylcoclaurine (HMC) producing reticuline. A 3D model of HOMT was constructed by homology modeling and further subjected to docking with its ligands and molecular dynamics simulations. The 3D structure of HOMT revealed unique structural features which permitted the methylation of HMC. The methylation of HMC was proposed to proceed by deprotonation of the 4'-hydroxyl group via His257 and Asp258 of HOMT, followed by a nucleophilic attack on the SAM-methyl group resulting in reticuline. HOMT showed high substrate specificity for methylation of HMC. The study evidenced that Gly117, Thr312 and Asp258 in HOMT might be the key residues for orienting substrate for specific catalysis.
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