Littlechild_2007_Biochem.Soc.Trans_35_1558

Reference

Title : Natural methods of protein stabilization: thermostable biocatalysts - Littlechild_2007_Biochem.Soc.Trans_35_1558
Author(s) : Littlechild JA , Guy J , Connelly S , Mallett L , Waddell S , Rye CA , Line K , Isupov M
Ref : Biochemical Society Transactions , 35 :1558 , 2007
Abstract :

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.

PubMedSearch : Littlechild_2007_Biochem.Soc.Trans_35_1558
PubMedID: 18031266

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Citations formats

Littlechild JA, Guy J, Connelly S, Mallett L, Waddell S, Rye CA, Line K, Isupov M (2007)
Natural methods of protein stabilization: thermostable biocatalysts
Biochemical Society Transactions 35 :1558

Littlechild JA, Guy J, Connelly S, Mallett L, Waddell S, Rye CA, Line K, Isupov M (2007)
Biochemical Society Transactions 35 :1558