Germacradienol synthase

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Germacradienol synthase
Identifiers
EC no. 4.2.3.22
CAS no. 211049-88-6
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Germacradienol synthase (EC 4.2.3.22, germacradienol/germacrene-D synthase, 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming). [1] [2] [3] This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate + H2O (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate

This enzyme requires Mg2+ for activity.

Related Research Articles

<span class="mw-page-title-main">Geosmin</span> Chemical compound responsible for the characteristic odour of earth

Geosmin ( jee-OZ-min) is an irregular sesquiterpenoid, produced from the universal sesquiterpene precursor farnesyl pyrophosphate (also known as farnesyl diphosphate), in a two-step Mg2+-dependent reaction. Geosmin, along with the irregular monoterpene 2-methylisoborneol, together account for the majority of biologically-caused taste and odor outbreaks in drinking water worldwide. Geosmin has a distinct earthy or musty odor, which most people can easily smell. The geosmin odor detection threshold in humans is very low, ranging from 0.006 to 0.01 micrograms per liter in water. Geosmin is also responsible for the earthy taste of beetroots and a contributor to the strong scent (petrichor) that occurs in the air when rain falls after a spell of dry weather or when soil is disturbed.

The enzyme (+)-δ-cadinene synthase catalyzes the chemical reaction

The enzyme aristolochene synthase catalyzes the chemical reaction

The enzyme germacrene-A synthase (EC 4.2.3.23) catalyzes the chemical reaction

The enzyme pentalenene synthase catalyzes the chemical reaction

The enzyme trichodiene synthase catalyzes the chemical reaction

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

Geosmin synthase or germacradienol-geosmin synthase designates a class of bifunctional enzymes that catalyze the conversion of farnesyl diphosphate (FPP) to geosmin, a volatile organic compound known for its earthy smell. The N-terminal half of the protein catalyzes the conversion of farnesyl diphosphate to germacradienol and germacrene D, followed by the C-terminal-mediated conversion of germacradienol to geosmin. The conversion of FPP to geosmin was previously thought to involve multiple enzymes in a biosynthetic pathway.

epi-Isozizaene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -epi-isozizaene-forming). This enzyme catalyses the following chemical reaction

Germacrene C synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (germacrene-C-forming). This enzyme catalyses the following chemical reaction

(+)-Epicubenol synthase (EC 4.2.3.64, farnesyl pyrophosphate cyclase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((+)-epicubenol-forming). This enzyme catalyses the following chemical reaction

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

Valencene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (valencene-forming). It is a terpene cyclase enzyme responsible for the biosynthesis of valencene, a sesquiterpene, using farnesyl pyrophosphate as its substrate. The first such enzyme was isolated using orange cDNA. This enzyme catalyses the following chemical reaction

(–)-Germacrene D synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -germacrene-D-forming). This enzyme catalyses the following chemical reaction

(+)-Germacrene D synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -germacrene-D-forming). This enzyme catalyses the following chemical reaction

exo-α-Bergamotene synthase (EC 4.2.3.81, trans-α-bergamotene synthase, LaBERS (gene)) is an enzyme with systematic name (2E,6E)-farnesyl diphosphate lyase (cyclizing, (–)-exo-α-bergamotene-forming). This enzyme catalyses the following chemical reaction:

7-epi-α-Selinene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (7-epi-α-selinene-forming). This enzyme catalyses the following chemical reaction

(+)-β-Caryophyllene synthase is an enzyme with systematic name (2Z,6E)-farnesyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction:

(–)-δ-Cadinene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

2-methylisoborneol synthase (EC 4.2.3.118, sco7700, 2-MIB cyclase, MIB synthase, MIBS) is an enzyme with systematic name (E)-2-methylgeranyl-diphosphate diphosphate-lyase (cyclizing, 2-methylisoborneol-forming). This enzyme catalyses the following chemical reaction

(E)-2-epi-β-Caryophyllene synthase (EC 4.2.3.137, (E)-2-epi-β-caryophyllene synthase, SmMTPSL26) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, (E)-2-epi-β-caryophyllene-forming). This enzyme catalyses the following chemical reaction

References

  1. ↑ Cane DE, Watt RM (February 2003). "Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis". Proceedings of the National Academy of Sciences of the United States of America. 100 (4): 1547–51. doi: 10.1073/pnas.0337625100 . PMC   149869 . PMID   12556563.
  2. ↑ He X, Cane DE (March 2004). "Mechanism and stereochemistry of the germacradienol/germacrene D synthase of Streptomyces coelicolor A3(2)". Journal of the American Chemical Society. 126 (9): 2678–9. doi:10.1021/ja039929k. PMID   14995166.
  3. ↑ Gust B, Challis GL, Fowler K, Kieser T, Chater KF (February 2003). "PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin". Proceedings of the National Academy of Sciences of the United States of America. 100 (4): 1541–6. doi: 10.1073/pnas.0337542100 . PMC   149868 . PMID   12563033.
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