Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution
Luo, Jinghui ; van Loo, Bert and Kamerlin, Shina C L LU
(2012)
In FEBS Letters
586(11).
p.30-1622
- Abstract
In recent years, it has become increasingly clear that many enzymes are catalytically "promiscuous". This can provide a springboard for protein evolution, allowing enzymes to acquire novel functionality without compromising their native activities. We present here a detailed study of Pseudomonas aeruginosa arylsulfatase (PAS), which catalyzes the hydrolysis of a number of chemically distinct substrates, with proficiencies comparable to that towards its native reaction. We demonstrate that the main driving force for the promiscuity is the ability to exploit the electrostatic preorganization of the active site for the native substrate, providing an example of chemistry-driven protein evolution.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/cc99be1a-2ab1-44d2-b82f-815f6ebabf92
- author
- Luo, Jinghui
; van Loo, Bert
and Kamerlin, Shina C L
LU
- publishing date
- 2012-06-04
- type
- Contribution to journal
- publication status
- published
- keywords
- Arylsulfatases/chemistry, Biocatalysis, Catalytic Domain, Evolution, Molecular, Hydrolysis, Models, Molecular, Molecular Weight, Phosphates/chemistry, Phosphoric Monoester Hydrolases/metabolism, Protons, Pseudomonas aeruginosa/enzymology, Static Electricity, Substrate Specificity
- in
- FEBS Letters
- volume
- 586
- issue
- 11
- pages
- 9 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:22673572
- scopus:84861637850
- ISSN
- 1873-3468
- DOI
- 10.1016/j.febslet.2012.04.012
- language
- English
- LU publication?
- no
- additional info
- Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
- id
- cc99be1a-2ab1-44d2-b82f-815f6ebabf92
- date added to LUP
- 2025-01-11 22:07:50
- date last changed
- 2025-04-06 11:26:37
@article{cc99be1a-2ab1-44d2-b82f-815f6ebabf92,
abstract = {{<p>In recent years, it has become increasingly clear that many enzymes are catalytically "promiscuous". This can provide a springboard for protein evolution, allowing enzymes to acquire novel functionality without compromising their native activities. We present here a detailed study of Pseudomonas aeruginosa arylsulfatase (PAS), which catalyzes the hydrolysis of a number of chemically distinct substrates, with proficiencies comparable to that towards its native reaction. We demonstrate that the main driving force for the promiscuity is the ability to exploit the electrostatic preorganization of the active site for the native substrate, providing an example of chemistry-driven protein evolution.</p>}},
author = {{Luo, Jinghui and van Loo, Bert and Kamerlin, Shina C L}},
issn = {{1873-3468}},
keywords = {{Arylsulfatases/chemistry; Biocatalysis; Catalytic Domain; Evolution, Molecular; Hydrolysis; Models, Molecular; Molecular Weight; Phosphates/chemistry; Phosphoric Monoester Hydrolases/metabolism; Protons; Pseudomonas aeruginosa/enzymology; Static Electricity; Substrate Specificity}},
language = {{eng}},
month = {{06}},
number = {{11}},
pages = {{30--1622}},
publisher = {{Wiley-Blackwell}},
series = {{FEBS Letters}},
title = {{Catalytic promiscuity in <i>Pseudomonas aeruginosa</i> arylsulfatase as an example of chemistry-driven protein evolution}},
url = {{http://dx.doi.org/10.1016/j.febslet.2012.04.012}},
doi = {{10.1016/j.febslet.2012.04.012}},
volume = {{586}},
year = {{2012}},
}