Target intelligence / Profile preview

Linalool synthase (LIS)

Target
LIS
Molecular classification
Enzyme, Lyase, Carbon-oxygen lyase, Terpene synthase
01

Overview

Linalool synthase is a member of the terpene synthase family responsible for the biosynthesis of the monoterpene alcohol linalool from geranyl diphosphate (GPP) [UniProt: Q9SPN0]. Found predominantly in plants, fungi, and some bacteria, this enzyme plays a pivotal role in producing volatile compounds that are essential for plant defense mechanisms against herbivores and for the attraction of pollinators [PubMed: 10450541]. The enzyme exists in different isoforms that stereospecifically produce either (3R)-linalool or (3S)-linalool, each contributing distinct aromatic properties to various essential oils, such as those from lavender, mint, and coriander [NCBI: PMC7020141]. In a clinical context, linalool synthase is not a human therapeutic target as it is not encoded by the human genome. However, it is a target of significant interest in metabolic engineering and synthetic biology for the bio-manufacturing of linalool, which is widely used in the fragrance and flavor industries [PubMed: 28628234]. While linalool itself has been studied for its potential pharmacological effects in humans—including sedative, anti-inflammatory, and analgesic properties mediated through GABAergic and NMDA receptor pathways—the synthase enzyme itself does not interact with any approved pharmaceutical drugs [PubChem: Linalool].

Other names
(3S)-linalool synthase(3R)-linalool synthaseGeranyl diphosphate linalooltransferaseS-linalool synthaseR-linalool synthaseLinalool lyase
02

Mechanism of action

Catalyzes the conversion of geranyl diphosphate (GPP) to linalool via the formation of a linalyl pyrophosphate intermediate or a direct carbocationic rearrangement followed by hydration [UniProt: Q9SPN0].

03

Biological functions

Secondary metabolismMonoterpenoid biosynthesisVolatile organic compound productionPlant defensePollinator attraction
04

Safety considerations

Not expressed in humans; no known human safety concerns related to enzyme inhibition or activation.

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