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Enzyme promiscuity: engine of evolutionary innovation.


ABSTRACT: Catalytic promiscuity and substrate ambiguity are keys to evolvability, which in turn is pivotal to the successful acquisition of novel biological functions. Action on multiple substrates (substrate ambiguity) can be harnessed for performance of functions in the cell that supersede catalysis of a single metabolite. These functions include proofreading, scavenging of nutrients, removal of antimetabolites, balancing of metabolite pools, and establishing system redundancy. In this review, we present examples of enzymes that perform these cellular roles by leveraging substrate ambiguity and then present the structural features that support both specificity and ambiguity. We focus on the phosphatases of the haloalkanoate dehalogenase superfamily and the thioesterases of the hotdog fold superfamily.

SUBMITTER: Pandya C 

PROVIDER: S-EPMC4215207 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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Enzyme promiscuity: engine of evolutionary innovation.

Pandya Chetanya C   Farelli Jeremiah D JD   Dunaway-Mariano Debra D   Allen Karen N KN  

The Journal of biological chemistry 20140910 44


Catalytic promiscuity and substrate ambiguity are keys to evolvability, which in turn is pivotal to the successful acquisition of novel biological functions. Action on multiple substrates (substrate ambiguity) can be harnessed for performance of functions in the cell that supersede catalysis of a single metabolite. These functions include proofreading, scavenging of nutrients, removal of antimetabolites, balancing of metabolite pools, and establishing system redundancy. In this review, we presen  ...[more]

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