Parallel molecular mechanisms for enzyme temperature adaptation-Reference-Cited by-同舟云学术

Parallel molecular mechanisms for enzyme temperature adaptation

Published:2021-03-05 Issue:6533 Volume:371 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Pinney Margaux M.¹^ORCID,Mokhtari Daniel A.¹^ORCID,Akiva Eyal²,Yabukarski Filip¹³^ORCID,Sanchez David M.⁴⁵^ORCID,Liang Ruibin⁴⁵^ORCID,Doukov Tzanko⁶^ORCID,Martinez Todd J.⁴⁵^ORCID,Babbitt Patricia C.²,Herschlag Daniel¹⁷⁸^ORCID

Affiliation:

1. Department of Biochemistry, Stanford University, Stanford, CA 94305, USA.

2. Department of Bioengineering and Therapeutic Sciences and Quantitative Biosciences Institute, University of California, San Francisco, CA 94158, USA.

3. Chan Zuckerberg Biohub, San Francisco, CA 94110, USA.

4. Department of Chemistry, Stanford University, Stanford, CA 94305, USA.

5. Department of Photon Sciences, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.

6. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.

7. Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA.

8. Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA.

Abstract

Some like it hot, others not Enzymes strike a delicate balance between features that enhance chemical reactivity and those that contribute to stable structure. Both features are important and can be unrelated or antagonistic. Pinney et al. combined rich experimental work on thermophilic and mesophilic variants of the enzyme ketosteroid isomerase (KSI) with bioinformatic data from a diverse set of bacterial enzymes to reveal the molecular determinants of thermal adaptation in enzymes. For KSI, they observed a trade-off between activity and thermal stability that comes down to a single active-site residue. With their larger dataset, they identified patterns of individual amino acid substitutions that are favored at higher temperatures, and also consider how networks of stabilizing interactions develop. Science , this issue p. eaay2784

Funder

National Science Foundation

National Institutes of Health

Joint Genome Institute

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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