Enzyme promiscuity: Engine of evolutionary innovation

Journal of Biological Chemistry

Volumn 289, Issue 44, 2014, Pages 30229-30236

  Pandya, Chetanya ^a   Farelli, Jeremiah D ^b   Dunaway Mariano, Debra ^c   Allen, Karen N ^a,b  

^a BOSTON UNIVERSITY   (United States)

^b USA   (United States)

^c UNIVERSITY OF NEW MEXICO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; METABOLITES;

BIOLOGICAL FUNCTIONS; EVOLUTIONARY INNOVATION; FOLD SUPERFAMILIES; METABOLITE POOLS; MULTIPLE SUBSTRATES; STRUCTURAL FEATURE; SYSTEM REDUNDANCY; THIOESTERASES;

SUBSTRATES;

ANTIMETABOLITE; ENZYME; HOLOALKANOATE DEHALOGENASE; HOTDOG FOLD THIOESTERASE; HOTDOG THIOESTERASE; PHOSPHATASE; PHOSPHOTRANSFERASE; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

ALPHA HELIX; BETA SHEET; BINDING SITE; CATALYSIS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HUMAN; HYDROGEN BOND; HYDROLYSIS; NONHUMAN; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN FAMILY; REVIEW; SUBSTRATE AMBIGUITY; ANIMAL; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; MOLECULAR EVOLUTION;

ANIMALS; BIOCATALYSIS; CATALYTIC DOMAIN; ENZYMES; EVOLUTION, MOLECULAR; HUMANS; MODELS, MOLECULAR; SUBSTRATE SPECIFICITY;

EID: 84908577179     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R114.572990     Document Type: Review

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