Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures.
Abstract
Random mutagenesis on thermophilic 3-isopropylmalate dehydrogenases (IPMDH; EC 1.1.1.85) produced mutant enzymes which adapt to low temperatures. These mutants had higher activity at lower temperatures than the wild-type enzyme without losing high thermostability. Here we report three structures of the mutants of Thermus thermophilus IPMDH determined by X-ray diffraction which was adapted to a low-temperature environment. Two of them have unstable coenzyme binding states and the other one probably has a stable substrate binding state. The present research suggests that the adaptation is correlated with the binding of either coenzyme or the substrate. Study holds ProTherm entries: 10880, 10881, 10882, 10883 Extra Details: cold-adapted mutants; 3-isopropylmalate dehydrogenase;,thermal stability; Thermus thermophilus; structural analysis
Submission Details
ID: Z87D8EFG3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:41 p.m.
Version: 1
Publication Details
Hirose R;Suzuki T;Moriyama H;Sato T;Yamagishi A;Oshima T;Tanaka N,Protein Eng. (2001) Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures. PMID:11297665Additional 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)