Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures.


Random mutagenesis on thermophilic 3-isopropylmalate dehydrogenases (IPMDH; EC 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


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:11297665
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 3-isopropylmalate dehydrogenase Q5SIY4 LEU3_THET8
99.4 3-isopropylmalate dehydrogenase P61494 LEU3_THET2
100.0 3-isopropylmalate dehydrogenase P61495 LEU3_THETH
91.9 3-isopropylmalate dehydrogenase P24098 LEU3_THEAQ