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Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution

Author

  • Jinghui Luo
  • Bert van Loo
  • Shina C L Kamerlin

Summary, in English

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.

Publishing year

2012-06-04

Language

English

Pages

30-1622

Publication/Series

FEBS Letters

Volume

586

Issue

11

Document type

Journal article

Publisher

Wiley-Blackwell

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

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-3468