Structure basis of the caffeic acid O-methyltransferase from Ligusiticum chuanxiong to understand its selective mechanism

Caffeic acid O-methyltransferase from Ligusticum chuanxiong (LcCOMT) showed strict regiospecificity despite a relative degree of preference. Compared with caffeic acid, methyl caffeate was the preferential substrate by its low Km and high Kcat. In this study, we obtained the SAM binary (1.80 Å) and...

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Veröffentlicht in:	International journal of biological macromolecules 2022-01, Vol.194, p.317-330
Hauptverfasser:	Song, Simin, Chen, Anqi, Zhu, Jianquan, Yan, Zicheng, An, Qiuju, Zhou, Jiayu, Liao, Hai, Yu, Yamei
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites Amino Acid Sequence caffeate O-methyltransferase caffeic acid Caffeic O-methyltransferase Catalysis Catalytic Domain hydrogen bonding Kinetics ligands Ligusticum - classification Ligusticum - enzymology Ligusticum - genetics Ligusticum sinense methylation Methyltransferases - chemistry Methyltransferases - genetics Models, Molecular Mutagenesis, Site-Directed mutation Phenols - chemistry Phylogeny Protein Conformation Recombinant Proteins regioselectivity Selective mechanism Structure-Activity Relationship Substrate Specificity tail X-ray structure
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