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Pure and Applied Chemistry

The Scientific Journal of IUPAC

Ed. by Burrows, Hugh / Weir, Ron / Stohner, Jürgen

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Mapping catalytic promiscuity in the alkaline phosphatase superfamily

Stefanie Jonas1 / Florian Hollfelder1

1Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, UK

Citation Information: Pure and Applied Chemistry. Volume 81, Issue 4, Pages 731–742, ISSN (Online) 1365-3075, ISSN (Print) 0033-4545, DOI: 10.1351/PAC-CON-08-10-20, January 2009

Publication History

Published Online:
2009-01-01

"Promiscuous" enzymes possess activities in addition to their native ones. Promiscuous activities could be remnants from an evolutionary ancestor that has been adapted to fulfil a new function following gene duplication. Alternatively, the observation of promiscuity could indicate that an enzyme has the potential to evolve into a new catalyst. Thus, the observation of promiscuity defines functional relationships in enzyme superfamilies. Crosswise promiscuity can provide an additional layer of connectivity between members of a - usually structurally defined - superfamily to establish a system for tracking the emergence and interconversion of enzymatic function. The systematic analysis of measured promiscuous rates may serve as a basis for drawing up phylogenetic relationships based on the potential for catalysis and may be useful for active use in directed evolution, suggesting evolutionary "short cuts". We review recent observations of catalytic promiscuity in members of the alkaline phosphatase (AP) superfamily that exhibit reciprocal relationships of crosswise promiscuity with rate accelerations (kcat/KM)/k2 between 106 and 1018. Specifically, we focus on the mechanistic features that appear to form the basis of catalytic promiscuity in this superfamily.

Keywords: catalytic promiscuity; enzymology; formylglycine; hydrolase; metalloenzyme; phosphate transfer; sulfate transfer; superfamily

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