EC Number   |
Protein Variants |
Reference |
|---|
  2.5.1.83 | A79F |
mutant enzyme subunit-A(wild-type)/subunit-B(A79L) shows 10fold increased Vmax-values and 11fold decreased Km-values for geranyl diphosphate, which becomes the most preferred substrate of the allylic primers. 5fold increase in KM-value for geranylgeranyl diphosphate. Mutation results in shortening the chain length of the major product. The major products are farnesylgeranyl diphosphate and geranylgeranyl diphosphate |
-, 702201 |
| 2.5.1.83 | A79L |
mutant enzyme subunit-A(wild-type)/subunit-B(A79L) shows 7fold increased Vmax-values and 6fold decreased Km-values for geranyl diphosphate, which becomes the most preferred substrate of the allylic primers. 3.9fold increase in KM-value for geranylgeranyl diphosphate. Mutation results in shortening the chain length of the major product. The major product is farnesylgeranyl diphosphate |
-, 702201 |
| 2.5.1.83 | more |
several amino acid residues in the larger subunits Bacillus subtilis heptaprenyl diphosphate synthase are selected for substitutions by site-directed mutagenesis and examined by combination with the corresponding wild type or mutated smaller subunits |
-, 702201 |
| 2.5.1.83 | V76G |
mutant enzyme subunit-A(wild-type)/subunit-B(V76G) gives octaprenyl diphosphate as the final products with farnesyl diphosphate as an allylic primer |
-, 702201 |
