A functional enzyme displays activity with at least one substrate and can be represented by a vector in substrate–activity space. Many enzymes, including GSTs (glutathione transferases), are promiscuous in the sense that they act on alternative substrates, and the corresponding vectors operate in multidimensional space. The direction of the vector is governed by the relative activities of the diverse substrates. Stochastic mutations of already existing enzymes generate populations of variants, and clusters of functionally similar mutants can serve as parents for subsequent generations of enzymes. The proper evolving unit is a functional quasi-species, which may not be identical with the ‘best’ variant in its generation. The manifestation of the quasi-species is dependent on the substrate matrix used to explore catalytic activities. Multivariate analysis is an approach to identifying quasi-species and to investigate evolutionary trajectories in the directed evolution of enzymes for novel functions.
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August 2009
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Conference Article|
July 22 2009
Multi-substrate–activity space and quasi-species in enzyme evolution: Ohno's dilemma, promiscuity and functional orthogonality
Bengt Mannervik;
Bengt Mannervik
1
1Department of Biochemistry and Organic Chemistry, Uppsala University, BMC 576, SE-75123 Uppsala, Sweden
1To whom correspondence should be addressed (email Bengt.Mannervik@biorg.uu.se).
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Arna Runarsdottir;
Arna Runarsdottir
1Department of Biochemistry and Organic Chemistry, Uppsala University, BMC 576, SE-75123 Uppsala, Sweden
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Sanela Kurtovic
Sanela Kurtovic
2
1Department of Biochemistry and Organic Chemistry, Uppsala University, BMC 576, SE-75123 Uppsala, Sweden
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Publisher: Portland Press Ltd
Received:
February 18 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (4): 740–744.
Article history
Received:
February 18 2009
Citation
Bengt Mannervik, Arna Runarsdottir, Sanela Kurtovic; Multi-substrate–activity space and quasi-species in enzyme evolution: Ohno's dilemma, promiscuity and functional orthogonality. Biochem Soc Trans 1 August 2009; 37 (4): 740–744. doi: https://doi.org/10.1042/BST0370740
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