Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
Pabis, Anna ; Duarte, Fernanda and Kamerlin, Shina C L LU
(2016)
In Biochemistry
55(22).
p.81-3061
- Abstract
The enzymes that facilitate phosphate and sulfate hydrolysis are among the most proficient natural catalysts known to date. Interestingly, a large number of these enzymes are promiscuous catalysts that exhibit both phosphatase and sulfatase activities in the same active site and, on top of that, have also been demonstrated to efficiently catalyze the hydrolysis of other additional substrates with varying degrees of efficiency. Understanding the factors that underlie such multifunctionality is crucial both for understanding functional evolution in enzyme superfamilies and for the development of artificial enzymes. In this Current Topic, we have primarily focused on the structural and mechanistic basis for catalytic promiscuity among... (More)
The enzymes that facilitate phosphate and sulfate hydrolysis are among the most proficient natural catalysts known to date. Interestingly, a large number of these enzymes are promiscuous catalysts that exhibit both phosphatase and sulfatase activities in the same active site and, on top of that, have also been demonstrated to efficiently catalyze the hydrolysis of other additional substrates with varying degrees of efficiency. Understanding the factors that underlie such multifunctionality is crucial both for understanding functional evolution in enzyme superfamilies and for the development of artificial enzymes. In this Current Topic, we have primarily focused on the structural and mechanistic basis for catalytic promiscuity among enzymes that facilitate both phosphoryl and sulfuryl transfer in the same active site, while comparing this to how catalytic promiscuity manifests in other promiscuous phosphatases. We have also drawn on the large number of experimental and computational studies of selected model systems in the literature to explore the different features driving the catalytic promiscuity of such enzymes. Finally, on the basis of this comparative analysis, we probe the plausible origins and determinants of catalytic promiscuity in enzymes that catalyze phosphoryl and sulfuryl transfer.
(Less)
- author
- Pabis, Anna
; Duarte, Fernanda
and Kamerlin, Shina C L
LU
- publishing date
- 2016-06-07
- type
- Contribution to journal
- publication status
- published
- keywords
- Animals, Catalysis, Catalytic Domain, Humans, Models, Molecular, Phosphates/metabolism, Phosphoric Monoester Hydrolases/metabolism, Protein Conformation, Substrate Specificity, Sulfatases/metabolism, Sulfates/metabolism
- in
- Biochemistry
- volume
- 55
- issue
- 22
- pages
- 21 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:27187273
- scopus:84973667758
- ISSN
- 0006-2960
- DOI
- 10.1021/acs.biochem.6b00297
- language
- English
- LU publication?
- no
- id
- 22cef52d-14f9-44db-a287-49e1c6dae247
- date added to LUP
- 2025-01-11 21:32:16
- date last changed
- 2025-01-21 03:19:57
@article{22cef52d-14f9-44db-a287-49e1c6dae247,
abstract = {{<p>The enzymes that facilitate phosphate and sulfate hydrolysis are among the most proficient natural catalysts known to date. Interestingly, a large number of these enzymes are promiscuous catalysts that exhibit both phosphatase and sulfatase activities in the same active site and, on top of that, have also been demonstrated to efficiently catalyze the hydrolysis of other additional substrates with varying degrees of efficiency. Understanding the factors that underlie such multifunctionality is crucial both for understanding functional evolution in enzyme superfamilies and for the development of artificial enzymes. In this Current Topic, we have primarily focused on the structural and mechanistic basis for catalytic promiscuity among enzymes that facilitate both phosphoryl and sulfuryl transfer in the same active site, while comparing this to how catalytic promiscuity manifests in other promiscuous phosphatases. We have also drawn on the large number of experimental and computational studies of selected model systems in the literature to explore the different features driving the catalytic promiscuity of such enzymes. Finally, on the basis of this comparative analysis, we probe the plausible origins and determinants of catalytic promiscuity in enzymes that catalyze phosphoryl and sulfuryl transfer.</p>}},
author = {{Pabis, Anna and Duarte, Fernanda and Kamerlin, Shina C L}},
issn = {{0006-2960}},
keywords = {{Animals; Catalysis; Catalytic Domain; Humans; Models, Molecular; Phosphates/metabolism; Phosphoric Monoester Hydrolases/metabolism; Protein Conformation; Substrate Specificity; Sulfatases/metabolism; Sulfates/metabolism}},
language = {{eng}},
month = {{06}},
number = {{22}},
pages = {{81--3061}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biochemistry}},
title = {{Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer}},
url = {{http://dx.doi.org/10.1021/acs.biochem.6b00297}},
doi = {{10.1021/acs.biochem.6b00297}},
volume = {{55}},
year = {{2016}},
}