Loganic acid O-methyltransferase (LAMT) (LAMT)

Loganic acid O-methyltransferase (LAMT) is a plant-derived enzyme, primarily characterized in Catharanthus roseus (Madagascar periwinkle), that plays a pivotal role in the biosynthesis of monoterpene indole alkaloids (MIAs) (UniProt B2KPR3). It belongs to the SABATH family of methyltransferases and catalyzes the S-adenosyl-L-methionine (SAM)-dependent methylation of loganic acid to produce loganin (PubMed: 18326827). This enzymatic step is a crucial gateway in the secoiridoid pathway, as loganin is the direct precursor to secologanin, which serves as the building block for over 2,000 different MIAs (PubMed: 29399933). Many of these alkaloids, such as vinblastine, vincristine, and ajmalicine, possess significant medicinal properties, particularly in oncology and cardiology (PubMed: 24104568). While LAMT is not a direct therapeutic target for human diseases, it is a major focus of biotechnological research aimed at metabolic engineering and the semi-synthetic production of high-value plant metabolites. The enzyme is highly specific for its substrate and is subject to feedback inhibition by its product, loganin, which helps regulate the flux of the alkaloid biosynthetic pathway (UniProt B2KPR3). Its structural and functional characterization has provided insights into the evolution of plant secondary metabolism and the development of biocatalysts for pharmaceutical synthesis (PubMed: 29399933).

Other names

Loganate O-methyltransferaseS-adenosyl-L-methionine:loganate 11-O-methyltransferaseLoganate methyltransferaseCrLAMT

Not applicable