CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.600 | Farnesyl Diphosphate Synthase | |
1.10.600.10 | Farnesyl Diphosphate Synthase |
Domain Context
CATH Clusters
Superfamily | Farnesyl Diphosphate Synthase |
Functional Family |
Enzyme Information
4.2.3.75 |
(-)-germacrene D synthase.
based on mapping to UniProt Q9X839
(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate.
-!- In Solidago canadensis the biosynthesis results in the pro-R hydrogen at C-1 of the farnesy diphosphate ending up at C-11 of the (-)- germacrene D. -!- With Streptomyces coelicolor the pro-S hydrogen at C-1 ends up at C-11 of the (-)-germacrene D. -!- Formerly EC 4.2.3.n13.
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4.1.99.16 |
Geosmin synthase.
based on mapping to UniProt Q9X839
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H(2)O = (-)-geosmin + acetone.
-!- Geosmin is the cause of the characteristic smell of moist soil. -!- It is a bifunctional enzyme. -!- The N-terminal part of the enzyme is EC 4.2.3.22, germacradienol synthase, and forms germacradienol from FPP. -!- The C-terminal part of the enzyme catalyzes the conversion of germacradienol to geosmin via (1S,4aS,8aS)-8,10-dimethyl- 1,2,3,4,4a,5,6,8a-octahydronaphthalene.
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4.2.3.22 |
Germacradienol synthase.
based on mapping to UniProt Q9X839
(2E,6E)-farnesyl diphosphate + H(2)O = (1E,4S,5E,7R)-germacra-1(10),5- dien-11-ol + diphosphate.
-!- H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. -!- Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. -!- Both products are formed from a common intermediate. -!- The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16), a widely occurring metabolite of many streptomycetes, bacteria and fungi. -!- Also catalyzes the reaction of EC 4.2.3.75.
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UniProtKB Entries (1)
Q9X839 |
CYC2_STRCO
Streptomyces coelicolor A3(2)
Germacradienol/geosmin synthase
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PDB Structure
PDB | 5DW7 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with alpha alpha Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence.
Biochemistry
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