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Title: Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure

Abstract

Enzymatic activity is crucial for various technological applications, yet the complex structures and limited stability of enzymes often hinder their use. Hence, de novo design of robust biocatalysts that are much simpler than their natural counterparts and possess enhanced catalytic activity has long been a goal in biotechnology. Here, we present evidence for the ability of a single amino acid to self-assemble into a potent and stable catalytic structural entity. Spontaneously, phenylalanine (F) molecules coordinate with zinc ions to form a robust, layered, supramolecular amyloid-like ordered architecture (F–Zn(ii)) and exhibit remarkable carbonic anhydrase-like catalytic activity. Furthermore, amongst the reported artificial biomolecular hydrolases, F–Zn(ii) displays the lowest molecular mass and highest catalytic efficiency, in addition to reusability, thermal stability, substrate specificity, stereoselectivity and rapid catalytic CO2 hydration ability. Thus, this report provides a rational path towards future de novo design of minimalistic biocatalysts for biotechnological and industrial applications.

Authors:
 [1];  [2]; ORCiD logo [1]; ORCiD logo [3];  [4];  [4]; ORCiD logo [2]; ORCiD logo [1]
  1. Tel Aviv Univ. (Israel)
  2. Univ. of California, Riverside, CA (United States)
  3. The Weizmann Inst. of Science, Rehovot (Israel)
  4. Univ. of California, Los Angeles, CA (United States). UCLA-DOE Inst. for Genomics and Proteomics
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE Office of Science (SC); National Institutes of Heath (NIH); European Research Commission (ERC); US Army Research Office (ARO)
OSTI Identifier:
1578238
Grant/Contract Number:  
694426; W911NF-17-1-0340; TG-ENG160024; P41 GM103403; AC02-06CH11357; S10 RR029205
Resource Type:
Accepted Manuscript
Journal Name:
Nature Catalysis
Additional Journal Information:
Journal Volume: 2; Journal Issue: 11; Journal ID: ISSN 2520-1158
Publisher:
Springer Nature
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Biocatalysis; bioinspired materials; biomimetics; heterogeneous catalysis; hydrolases

Citation Formats

Makam, Pandeeswar, Yamijala, Sharma C., Tao, Kai, Shimon, Linda W., Eisenberg, David S., Sawaya, Michael R., Wong, Bryan M., and Gazit, Ehud. Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure. United States: N. p., 2019. Web. doi:10.1038/s41929-019-0348-x.
Makam, Pandeeswar, Yamijala, Sharma C., Tao, Kai, Shimon, Linda W., Eisenberg, David S., Sawaya, Michael R., Wong, Bryan M., & Gazit, Ehud. Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure. United States. https://doi.org/10.1038/s41929-019-0348-x
Makam, Pandeeswar, Yamijala, Sharma C., Tao, Kai, Shimon, Linda W., Eisenberg, David S., Sawaya, Michael R., Wong, Bryan M., and Gazit, Ehud. Mon . "Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure". United States. https://doi.org/10.1038/s41929-019-0348-x. https://www.osti.gov/servlets/purl/1578238.
@article{osti_1578238,
title = {Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure},
author = {Makam, Pandeeswar and Yamijala, Sharma C. and Tao, Kai and Shimon, Linda W. and Eisenberg, David S. and Sawaya, Michael R. and Wong, Bryan M. and Gazit, Ehud},
abstractNote = {Enzymatic activity is crucial for various technological applications, yet the complex structures and limited stability of enzymes often hinder their use. Hence, de novo design of robust biocatalysts that are much simpler than their natural counterparts and possess enhanced catalytic activity has long been a goal in biotechnology. Here, we present evidence for the ability of a single amino acid to self-assemble into a potent and stable catalytic structural entity. Spontaneously, phenylalanine (F) molecules coordinate with zinc ions to form a robust, layered, supramolecular amyloid-like ordered architecture (F–Zn(ii)) and exhibit remarkable carbonic anhydrase-like catalytic activity. Furthermore, amongst the reported artificial biomolecular hydrolases, F–Zn(ii) displays the lowest molecular mass and highest catalytic efficiency, in addition to reusability, thermal stability, substrate specificity, stereoselectivity and rapid catalytic CO2 hydration ability. Thus, this report provides a rational path towards future de novo design of minimalistic biocatalysts for biotechnological and industrial applications.},
doi = {10.1038/s41929-019-0348-x},
journal = {Nature Catalysis},
number = 11,
volume = 2,
place = {United States},
year = {Mon Sep 23 00:00:00 EDT 2019},
month = {Mon Sep 23 00:00:00 EDT 2019}
}

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Works referencing / citing this record:

A minimalistic hydrolase based on co-assembled cyclic dipeptides
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