EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
- |
Streptomyces coelicolor |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
- |
Sorangium cellulosum |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
- |
Aphanizomenon gracile |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
- |
Sorangium cellulosum Soce56 |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
- |
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
- |
Aphanizomenon gracile WH-1 |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O |
catalysed by the C-terminal domain of the bifunctional enzyme |
Streptomyces coelicolor |
(-)-geosmin + acetone |
- |
? |
| 4.1.99.16 | more |
conversion of germacradienol to geosmin results in the release of the three-carbon side chain as acetone and involves a 1,2-hydride shift of the bridgehead hydrogen exclusively into ring B of geosmin |
Streptomyces coelicolor |
? |
- |
? |
| 4.1.99.16 | more |
geosmin synthase from Streptomyces coelicolor (ScGS) catalyzes an unusual, metal-dependent terpenoid cyclization and fragmentation reaction sequence. Two distinct active sites are required for catalysis: the N-terminal domain catalyzes the ionization and cyclization of farnesyl diphosphate to form germacradienol and inorganic pyrophosphate (PPi), and the C-terminal domain catalyzes the protonation, cyclization, and fragmentation of germacradienol to form geosmin and acetone through a retro-Prins reaction. The enzyme has an alpha,alpha domain architecture, each domain contains the metal-binding motifs typical of a class I terpenoid cyclase, and each domain requires Mg2+ for catalysis. There is no direct channel for transfer of the intermediate from the active site of the N-terminal domain to that of the C-terminal domain. It is a diiffusive transfer of the germacradienol intermediate |
Streptomyces coelicolor |
? |
- |
? |
| 4.1.99.16 | more |
geosmin synthase from Streptomyces coelicolor (ScGS) catalyzes an unusual, metal-dependent terpenoid cyclization and fragmentation reaction sequence. Two distinct active sites are required for catalysis: the N-terminal domain catalyzes the ionization and cyclization of farnesyl diphosphate to form germacradienol and inorganic pyrophosphate (PPi), and the C-terminal domain catalyzes the protonation, cyclization, and fragmentation of germacradienol to form geosmin and acetone through a retro-Prins reaction. The enzyme has an alpha,alpha domain architecture, each domain contains the metal-binding motifs typical of a class I terpenoid cyclase, and each domain requires Mg2+ for catalysis. There is no direct channel for transfer of the intermediate from the active site of the N-terminal domain to that of the C-terminal domain. It is a diiffusive transfer of the germacradienol intermediate |
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 |
? |
- |
? |
