Sabinene-hydrate synthase

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sabinene-hydrate synthase
Identifiers
EC no. 4.2.3.11
CAS no. 166800-09-5
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ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
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Gene Ontology AmiGO / QuickGO
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The enzyme sabinene-hydrate synthase (EC 4.2.3.11) catalyzes the chemical reaction

geranyl diphosphate + H2O sabinene hydrate + 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 (cyclizing, sabinene-hydrate-forming). This enzyme is also called sabinene hydrate cyclase. This enzyme participates in monoterpenoid biosynthesis.

Related Research Articles

<span class="mw-page-title-main">Sabinene</span> Chemical compound

Sabinene is a natural bicyclic monoterpene with the molecular formula C10H16. It is isolated from the essential oils of a variety of plants including Marjoram, holm oak (Quercus ilex) and Norway spruce (Picea abies). It has a strained ring system with a cyclopentane ring fused to a cyclopropane ring.

<span class="mw-page-title-main">Bornyl diphosphate synthase</span>

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 aristolochene 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 taxadiene synthase catalyzes the chemical reaction

The enzyme monoterpenyl-diphosphatase (EC 3.1.7.3) catalyzes the reaction

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

Patchoulol synthase (EC 4.2.3.70) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming). This enzyme catalyses the following chemical reaction

(+)-Car-3-ene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-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

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

(+)-Sabinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-sabinene-forming]. This enzyme catalyses the following chemical reaction

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

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

(+)-camphene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-camphene-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

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

References


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