Article
An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily.
Proceedings of the National Academy of Sciences of the United States of America - 16 Feb 2010
van Loo Bert, Jonas Stefanie, Babtie Ann C, Benjdia Alhosna, Berteau Olivier, Hyvönen Marko, Hollfelder Florian
Abstract excerpt
We report a catalytically promiscuous enzyme able to efficiently promote the hydrolysis of six different substrate classes. Originally assigned as a phosphonate monoester hydrolase (PMH) this enzyme exhibits substantial second-order rate accelerations ((k(cat)/K(M))/k(w)), ranging from 10(7) to as high as 10(19), for the hydrolyses of phosphate mono-, di-, and triesters, phosphonate monoesters, sulfate...
Topics
- Alkaline Phosphatase
- Burkholderia
- Catalysis
- Catalytic Domain
- Chromatography, Gel
- Evolution, Molecular
- Hydrogen-Ion Concentration
- Hydrolases
- Models, Molecular
- Molecular Structure