The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase.
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 degrees C when compared with the wild-type IPMDH. Study holds ProTherm entries: 22914, 22915, 22916, 22917 Extra Details: 0.5 mM EDTA was added in the experiment Ancestral residue; Protein stability; 3-Isopropylmalate dehydrogenase; Thermus thermophilus
Submission Details
ID: PVqRqV6H3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:54 p.m.
Version: 1
Publication Details
Watanabe K;Yamagishi A,FEBS Lett. (2006) The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase. PMID:16797545Additional Information
Study Summary
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)
Correlation with other assays (exact sequence matches)
Relevant PDB Entries
| Structure ID | Release Date | Resolution | Structure Title |
|---|---|---|---|
| 1WAL | 1999-05-17T00:00:00+0000 | 2.27 | 3-ISOPROPYLMALATE DEHYDROGENASE (IPMDH) MUTANT (M219A)FROM THERMUS THERMOPHILUS |
| 1DPZ | 1999-12-29T00:00:00+0000 | 2.8 | STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD711 |
| 1DR0 | 2000-01-06T00:00:00+0000 | 2.2 | STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD708 |
| 1DR8 | 2000-01-06T00:00:00+0000 | 2.7 | STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177 |
| 1G2U | 2000-10-21T00:00:00+0000 | 2.1 | THE STRUCTURE OF THE MUTANT, A172V, OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THERMUS THERMOPHILUS HB8 : ITS THERMOSTABILITY AND STRUCTURE. |
| 1GC8 | 2000-07-27T00:00:00+0000 | 2.5 | THE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 3-ISOPROPYLMALATE DEHYDROGENASE MUTATED AT 172TH FROM ALA TO PHE |
| 1GC9 | 2000-07-28T00:00:00+0000 | 2.3 | THE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 3-ISOPROPYLMALATE DEHYDROGENASE MUTATED AT 172TH FROM ALA TO GLY |
| 1HEX | 1994-09-09T00:00:00+0000 | 2.5 | STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE IN COMPLEX WITH NAD+: LIGAND-INDUCED LOOP-CLOSING AND MECHANISM FOR COFACTOR SPECIFICITY |
| 1IDM | 1995-05-19T00:00:00+0000 | 2.2 | 3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA |
| 1IPD | 1992-01-29T00:00:00+0000 | 2.2 | THREE-DIMENSIONAL STRUCTURE OF A HIGHLY THERMOSTABLE ENZYME, 3-ISOPROPYLMALATE DEHYDROGENASE OF THERMUS THERMOPHILUS AT 2.2 ANGSTROMS RESOLUTION |