Pressure-induced activation and pressure-tolerance of mutated thermolysin at 119

Autor:	Satoshi Fujiwara, Satoshi Hanzawa, Shun-ichi Kidokoro, Kimiko Endo, Shigeru Kunugi
Rok vydání:	2000
Předmět:	chemistry.chemical_classification In situ Enzyme chemistry Transition (genetics) Stereochemistry Thermolysin Point mutation Mole Mutant Wild type Condensed Matter Physics Molecular biology
Zdroj:	High Pressure Research. 19:241-245
ISSN:	1477-2299 0895-7959
DOI:	10.1080/08957950008202560
Popis:	The pressure activation of thermolysin substitution at the 119th site was studied for four mutants and the wild type (Q119Q. Q119N, Q119R, Q119E and Q119D). The highest activation recorded over 30 fold and the activation volumes (ΔV‡) were about -75ml/mol for Q119Q, Q119N and Q119R, while Q119E and Q119D showed only a10 fold activation and ΔV‡ of around -6Oml/mol. The pressure-tolerance of these enzymes were investigated through the in situ observation of their intrinsic fluorescence. Q119E and Q119D showed smaller ΔG app and ΔG app of transition than the wild type.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::a590cb45eaae749ce009510837bb18e1 https://doi.org/10.1080/08957950008202560 Zobrazit plný text záznamu