Drastic changes in the substrate specificity of geranylgeranyl diphosphate synthase from Sulfolobus acidocaldarius by a single amino acid substitution

Autor:	Takeshi Nakamura, Masahiko Nagaki, Norimasa Ohya
Rok vydání:	2012
Předmět:	Sulfolobus acidocaldarius Serine chemistry.chemical_compound Biochemistry ATP synthase biology chemistry Prenylation Glycine Prenyltransferase biology.protein Phenylalanine Substrate analog
Zdroj:	Transactions of the Materials Research Society of Japan. 37:325-328
ISSN:	2188-1650 1382-3469
Popis:	Geranylgeranyl diphosphate (GGPP) synthase catalyzes the condensation of isopentenyl diphosphate with dimethylallyl diphosphate, geranyl diphosphate or farnesyl diphosphate to produce GGPP as the final product. GGPP synthase in the thermophilic bacterium Sulfolobus acidocaldarius can hardly accept substrate analogs possessing oxygen atoms in their prenyl chains. We have prepared several point-mutated S. acidocaldarius GGPP synthases in which phenylalanine was substituted with glycine (F77G) or serine (F77S). Interestingly, the reactivity of the mutated GGPP synthase was enhanced with respect to substrate analogs possessing ωoxygen atoms in their prenyl chains.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::7b096154e7cb318d1ac6ddac39ed3cd0 https://doi.org/10.14723/tmrsj.37.325 Zobrazit plný text záznamu