Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily
Pabis, Anna and Kamerlin, Shina Caroline Lynn LU
(2016)
In Current Opinion in Structural Biology
37.
p.14-21
- Abstract
Catalytic promiscuity, that is, the ability of single enzymes to facilitate the turnover of multiple, chemically distinct substrates, is a widespread phenomenon that plays an important role in the evolution of enzyme function. Additionally, such pre-existing multifunctionality can be harnessed in artificial enzyme design. The members of the alkaline phosphatase superfamily have served extensively as both experimental and computational model systems for enhancing our understanding of catalytic promiscuity. In this Opinion, we present key recent computational studies into the catalytic activity of these highly promiscuous enzymes, highlighting the valuable insight they have provided into both the molecular basis for catalytic promiscuity... (More)
Catalytic promiscuity, that is, the ability of single enzymes to facilitate the turnover of multiple, chemically distinct substrates, is a widespread phenomenon that plays an important role in the evolution of enzyme function. Additionally, such pre-existing multifunctionality can be harnessed in artificial enzyme design. The members of the alkaline phosphatase superfamily have served extensively as both experimental and computational model systems for enhancing our understanding of catalytic promiscuity. In this Opinion, we present key recent computational studies into the catalytic activity of these highly promiscuous enzymes, highlighting the valuable insight they have provided into both the molecular basis for catalytic promiscuity in general, and its implications for the evolution of phosphatase activity.
(Less)
- author
- Pabis, Anna
and Kamerlin, Shina Caroline Lynn
LU
- publishing date
- 2016-04
- type
- Contribution to journal
- publication status
- published
- keywords
- Alkaline Phosphatase/chemistry, Catalysis, Catalytic Domain, Static Electricity, Structure-Activity Relationship
- in
- Current Opinion in Structural Biology
- volume
- 37
- pages
- 8 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:26716576
- scopus:84950324469
- ISSN
- 1879-033X
- DOI
- 10.1016/j.sbi.2015.11.008
- language
- English
- LU publication?
- no
- additional info
- Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.
- id
- e556a084-2748-472e-9011-77089551ff42
- date added to LUP
- 2025-01-11 21:34:00
- date last changed
- 2025-06-15 16:06:48
@article{e556a084-2748-472e-9011-77089551ff42,
abstract = {{<p>Catalytic promiscuity, that is, the ability of single enzymes to facilitate the turnover of multiple, chemically distinct substrates, is a widespread phenomenon that plays an important role in the evolution of enzyme function. Additionally, such pre-existing multifunctionality can be harnessed in artificial enzyme design. The members of the alkaline phosphatase superfamily have served extensively as both experimental and computational model systems for enhancing our understanding of catalytic promiscuity. In this Opinion, we present key recent computational studies into the catalytic activity of these highly promiscuous enzymes, highlighting the valuable insight they have provided into both the molecular basis for catalytic promiscuity in general, and its implications for the evolution of phosphatase activity.</p>}},
author = {{Pabis, Anna and Kamerlin, Shina Caroline Lynn}},
issn = {{1879-033X}},
keywords = {{Alkaline Phosphatase/chemistry; Catalysis; Catalytic Domain; Static Electricity; Structure-Activity Relationship}},
language = {{eng}},
pages = {{14--21}},
publisher = {{Elsevier}},
series = {{Current Opinion in Structural Biology}},
title = {{Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily}},
url = {{http://dx.doi.org/10.1016/j.sbi.2015.11.008}},
doi = {{10.1016/j.sbi.2015.11.008}},
volume = {{37}},
year = {{2016}},
}