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Photo Lynn Kamerlin

Lynn Kamerlin

Professor

Photo Lynn Kamerlin

Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily

Author

  • Anna Pabis
  • Shina Caroline Lynn Kamerlin

Summary, in English

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.

Publishing year

2016-04

Language

English

Pages

14-21

Publication/Series

Current Opinion in Structural Biology

Volume

37

Document type

Journal article review

Publisher

Elsevier

Keywords

  • Alkaline Phosphatase/chemistry
  • Catalysis
  • Catalytic Domain
  • Static Electricity
  • Structure-Activity Relationship

Status

Published

ISBN/ISSN/Other

  • ISSN: 1879-033X