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The influence of dipeptide composition on optimum temperature of alcohol dehydrogenase

Paper ID Volume ID Publish Year Pages File Format Full-Text
18525 42725 2006 6 PDF Available
Title
The influence of dipeptide composition on optimum temperature of alcohol dehydrogenase
Abstract

A stepwise regression method was used to search the dipeptides responsible for the optimum temperature (Topt) of alcohol dehydrogenase, for dipeptides can provide position information of the related residues for rational protein mutation. It was found that the positive dipeptides were RA, GP, GE and LP whereas the negative dipeptides were DD, HQ, PC, QV, YN, DP, QQ, RI, NA and GN. The calculated temperature fitted the experimental optimum temperature of the alcohol dehydrogenase very well and the mean absolute error was only 4.33 °C. Using the known crystal structure of alcohol dehydrogenase, we found that most of the positive dipeptides were located in the α-helix, while the negative ones were in the β-sheet, turn or the coil. The thermostable mechanism was discussed and the result obtained could be helpful to engineer alcohol dehydrogenase with high temperature activity.

Keywords
ADH, alcohol dehydrogenase; SDM, site-directed mutagenesis; Topt, optimum temperature; Tpre, temperature calculated from the stepwise regressionAlcohol dehydrogenase; Dipeptide composition; Stepwise regression; Thermostability
First Page Preview
The influence of dipeptide composition on optimum temperature of alcohol dehydrogenase
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 4, 2 August 2006, Pages 811–816
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering