Natural methods of protein stabilization: thermostable biocatalysts.
Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They have important use in these industries due to their increased stability which is often required during commercial reaction conditions. The approach used in these studies is to learn how nature has managed to stabilize these proteins using a detailed knowledge of their biochemical properties and three-dimensional structures. This is illustrated with several different classes of enzyme that have been studied at Exeter. These include alcohol dehydrogenase, aminoacylase, pyroglutamyl carboxypeptidase, gamma-lactamase, dehalogenase and lysophospholipase.
Littlechild
J A
JA
School of Biosciences, Henry Wellcome Building for Biocatalysis, University of Exeter, Stocker Road, Exeter EX4 4QD, U.K. J.A.Littlechild@ex.ac.uk
Guy
J
J
Connelly
S
S
Mallett
L
L
Waddell
S
S
Rye
C A
CA
Line
K
K
Isupov
M
M
D000426:Alcohol Dehydrogenase / Q000737:chemistry; D000581:Amidohydrolases / Q000737:chemistry; D002268:Carboxypeptidases / Q000737:chemistry; D002384:Catalysis; D006867:Hydrolases / Q000737:chemistry; D008245:Lysophospholipase / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D013696:Temperature
D011506:Proteins; D000426:Alcohol Dehydrogenase; D006867:Hydrolases; D008245:Lysophospholipase; D002268:Carboxypeptidases; D000581:Amidohydrolases; C019672:aminoacylase I; C401943:gamma-lactamase