Carboxylic ester hydrolases from hyperthermophiles.
Carboxylic ester hydrolyzing enzymes constitute a large group of enzymes that are able to catalyze the hydrolysis, synthesis or transesterification of an ester bond. They can be found in all three domains of life, including the group of hyperthermophilic bacteria and archaea. Esterases from the latter group often exhibit a high intrinsic stability, which makes them of interest them for various biotechnological applications. In this review, we aim to give an overview of all characterized carboxylic ester hydrolases from hyperthermophilic microorganisms and provide details on their substrate specificity, kinetics, optimal catalytic conditions, and stability. Approaches for the discovery of new carboxylic ester hydrolases are described. Special attention is given to the currently characterized hyperthermophilic enzymes with respect to their biochemical properties, 3D structure, and classification.
Levisson
Mark
M
Department of Agrotechnology and Food Sciences, Wageningen University, The Netherlands. mark.levisson@wur.nl
van der Oost
John
J
Kengen
Servé W M
SW
D001105:Archaea / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology; D001709:Biotechnology / Q000379:methods; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000502:physiology*; D004798:Enzymes / Q000502:physiology; D004952:Esters / Q000737:chemistry; D016678:Genome; D006358:Hot Temperature; D006868:Hydrolysis; D008954:Models, Biological; D008956:Models, Chemical; D008968:Molecular Conformation; D016366:Open Reading Frames; D013379:Substrate Specificity; D013696:Temperature
D004798:Enzymes; D004952:Esters; D002265:Carboxylic Ester Hydrolases