Myrcene synthase

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myrcene synthase
Identifiers
EC no. 4.2.3.15
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BRENDA BRENDA entry
ExPASy NiceZyme view
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MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
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NCBI proteins

The enzyme myrcene synthase (EC 4.2.3.15) catalyzes the chemical reaction

geranyl diphosphate myrcene + diphosphate

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is geranyl-diphosphate diphosphate-lyase (myrcene-forming). This enzyme participates in monoterpenoid biosynthesis.

Related Research Articles

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In enzymology, bornyl diphosphate synthase (BPPS) (EC 5.5.1.8) is an enzyme that catalyzes the chemical reaction

The enzyme (4S)-limonene synthase catalyzes the chemical reaction

The enzyme (–)-endo-Fenchol synthase (EC 4.2.3.10) catalyzes the chemical reaction

In enzymology, a pinene synthase is an enzyme that catalyzes the chemical reaction

The enzyme (R)-limonene synthase (EC 4.2.3.20) catalyzes the reversible chemical reaction

The enzyme R-linalool synthase (EC 4.2.3.26) catalyzes the chemical reaction

The enzyme sabinene-hydrate synthase (EC 4.2.3.11) catalyzes the chemical reaction

The enzyme S-linalool synthase (EC 4.2.3.25) catalyzes the chemical reaction

<span class="mw-page-title-main">Terpene synthase N terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the N terminal domain of the TPS protein.

<span class="mw-page-title-main">Terpene synthase C terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the C terminal domain of the TPS protein.

β-Phellandrene synthase (neryl-diphosphate-cyclizing) is an enzyme with systematic name neryl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

β-Phellandrene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

Geranyl-diphosphate diphosphate-lyase may refer to:

Tricyclene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(E)-β-Ocimene synthase (EC 4.2.3.106, β-ocimene synthase, AtTPS03, ama0a23, LjEbetaOS, MtEBOS) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase ((E)-β-ocimene-forming). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">1,8-cineole synthase</span>

1,8-Cineole synthase (EC 4.2.3.108, 1,8-cineole cyclase, geranyl pyrophoshate:1,8-cineole cyclase, 1,8-cineole synthetase) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming). This enzyme catalyses the following chemical reaction

(–)-α-Terpineol synthase (EC 4.2.3.111) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-α-terpineol-forming]. This enzyme catalyses the following chemical reaction

(+)-α-Terpineol synthase (EC 4.2.3.112) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-terpineol-forming]. This enzyme catalyses the following chemical reaction

(–)-α-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(–)-β-Pinene synthase (EC 4.2.3.120, β-geraniolene synthase, (–)-(1S,5S)-pinene synthase, geranyldiphosphate diphosphate lyase (pinene forming)) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-β-pinene-forming]. This enzyme catalyses the following chemical reaction

References


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