2.5.1.83: hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
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For detailed information about hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific], go to the full flat file.
Reaction
Synonyms
C30PP synthase, COQ1, Coq1p, EC 2.5.1.33, hexaprenyl pyrophosphate synthetase, hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific], HexPP synthase, HexPPs, HexPS
ECTree
2.5.1.83 hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]Advanced search results
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results (Engineering
Engineering on EC 2.5.1.83 - hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
V76G
mutant enzyme subunit-A(wild-type)/subunit-B(V76G) gives octaprenyl diphosphate as the final products with farnesyl diphosphate as an allylic primer
A79F
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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
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A79L
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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
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V76G
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mutant enzyme subunit-A(wild-type)/subunit-B(V76G) gives octaprenyl diphosphate as the final products with farnesyl diphosphate as an allylic primer
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additional information
additional information
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
additional information
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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
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