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The role of histidine‐114 of Sulfolobus acidocaldarius geranylgeranyl diphosphate synthase in chain‐length determination
Author(s) -
Hirooka Kazutake,
Kato Tatsuya,
Matsu-ura Jun-ichiro,
Hemmi Hisashi,
Nishino Tokuzo
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01972-4
Subject(s) - sulfolobus acidocaldarius , prenylation , prenyltransferase , biochemistry , sulfolobus , atp synthase , histidine , chemistry , mutant , stereochemistry , enzyme , archaea , gene
Sulfolobus acidocaldarius geranylgeranyl diphosphate synthase yields (all‐ E )‐C 20 prenyl diphosphate as a final product. The three‐dimensional model of the enzyme suggested that removing two bulky residues at 77 and 114 would allow additional prenyl‐chain elongation. To test this, we examined several mutants with substitutions at 77 and/or 114. As a result, the mutants, F77G, F77G and H114A, F77G and H114G, H114A, and H114G gave C 30 , C 45 , C 50 , C 30 and C 40 as the main long product, respectively. These observations indicate that histidine‐114 plays a crucial role in chain‐length determination along with phenylalanine‐77.