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<< < Results 11 - 20 of 24 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30K130I mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type 637629
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30L94S 9fold lower Vmax values and 7fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme 637629
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30more elucidation of the mechanism of chain length determination of Bacillus stearothermophilus HepPS by site-directed mutagenesis 637630
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30more 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
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30more the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases 637628
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30more the hybrid-type combination of component I (Bacillus subtilis) and component II' (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus 637631
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30N127A mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type 637629
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30S80F single replacement to the aromatic residue at the fourth or the fifth position before the first aspartate-rich motif (FARM), mainly yields a C20 product 637630
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30T76V mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type 637629
Show all pathways known for 2.5.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.30V76I mutant enzyme subunit-I(wild-type)/subunit-II(A79L), octaprenyl diphosphate is the final product with farnesyl diphosphate as allylic primer 702201
<< < Results 11 - 20 of 24 > >>