The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase
In: FEBS Letters, Jg. 580 (2006-07-10), Heft 16, S. 3867-3871
Online
academicJournal
Zugriff:
Abstract: Previously, we showed that mutants of Thermus thermophilus 3-isopropylmalate dehydrogenase (IPMDH) each containing a residue (ancestral residue) that had been predicted to exist in a postulated common ancestor protein often have greater thermal stabilities than does the contemporary wild-type enzyme. In this study, the combined effects of multiple ancestral residues were analyzed. Two mutants, containing multiple mutations, Sup3mut (Val181Thr/Pro324Thr/Ala335Glu) and Sup4mut (Leu134Asn/Val181Thr/Pro324Thr/Ala335Glu) were constructed and show greater thermal stabilities than the wild-type and single-point mutant IPMDHs do. Most of the mutants have similar or improved catalytic efficiencies at 70°C when compared with the wild-type IPMDH. [Copyright &y& Elsevier]
Titel: |
The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase
|
---|---|
Autor/in / Beteiligte Person: | Watanabe, Keiko ; Yamagishi, Akihiko |
Link: | |
Zeitschrift: | FEBS Letters, Jg. 580 (2006-07-10), Heft 16, S. 3867-3871 |
Veröffentlichung: | 2006 |
Medientyp: | academicJournal |
ISSN: | 0014-5793 (print) |
DOI: | 10.1016/j.febslet.2006.06.012 |
Schlagwort: |
|
Sonstiges: |
|