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

Pandeeswar Makam, Sharma S.R.K.C. Yamijala, Kai Tao, Linda J.W. Shimon, David S. Eisenberg, Michael R. Sawaya, Bryan M. Wong, Ehud Gazit

Research output: Contribution to journalArticlepeer-review

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. Notably, 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.

Original languageEnglish
Pages (from-to)977-985
Number of pages9
JournalNature Catalysis
Volume2
Issue number11
DOIs
StatePublished - 1 Nov 2019

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