View source for PMID:20585771

{{RightTOC}}

<!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.2791.W4ee7ff5cbc884-->
<!--
******************************************************************************************
* 
*   ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. ** 
* 
****************************************************************************************** -->
{|   id="W4ee7ff5cbc884"  class=" tableEdit PMID_info_table"  

|-
!align=left  |Citation
||
'''Zhang, H, Lountos, GT, Ching, CB and Jiang, R'''  (2010) Engineering of glycerol dehydrogenase for improved activity towards 1, 3-butanediol.''Appl. Microbiol. Biotechnol.'' '''88''':117-24
|-
!align=left  |Abstract
||
The objective of this study was to use protein engineering techniques to enhance the catalytic activity of glycerol dehydrogenase (GlyDH) on racemic 1, 3-butanediol (1, 3-BDO) for the bioproduction of the important pharmaceutical intermediate 4-hydroxy-2-butanone. Three GlyDH genes (gldA) from Escherichia coli K-12, Salmonella enterica, and Klebsiella pneumoniae MGH78578 were shuffled to generate a random mutagenesis library. The nitroblue tetrazolium/phenazine methosulfate high throughput screening protocol was used to select four chimeric enzymes with up to a 2.6-fold improved activity towards 1, 3-BDO. A rational design method was also employed to further improve the enzyme activity after DNA shuffling. Based on the homology model of GlyDH (Escherichia coli), Asp121 was predicted to influence 1, 3-BDO binding and replaced with Ala by site-directed mutagenesis. Combination of the mutations from both DNA shuffling and rational design produced the best mutant with a V (max) value of 126.6 U/mg, a 26-fold activity increase compared with that of the wild type GlyDH from E. coli.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20585771 PubMed]
Online version:[http://dx.doi.org/10.1007/s00253-010-2735-8 10.1007/s00253-010-2735-8]
|-
!align=left  |Keywords
||
Butylene Glycols; DNA Shuffling; DNA, Bacterial; Escherichia coli K12; Hydroxybutyrates; Klebsiella pneumoniae; Methylphenazonium Methosulfate; Nitroblue Tetrazolium; Protein Engineering; Salmonella enterica; Sugar Alcohol Dehydrogenases

|- class="tableEdit_footer" 
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=2ccfb3c7bf1208312f02a69e64bfd9e0.2791.W4ee7ff5cbc884&page=2791&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
<!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.2791.W4ee7ff5cbc884-->

==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect><!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.2791.D4ee7ff5d080dc-->
<!--
******************************************************************************************
* 
*   ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. ** 
* 
****************************************************************************************** -->
{|   id="D4ee7ff5d080dc"  class=" tableEdit Phenotype_Table_2"  
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer" 
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=2ccfb3c7bf1208312f02a69e64bfd9e0.2791.D4ee7ff5d080dc&page=2791&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table]</span> || || || || || || || || ||
|}
<!--box uid=2ccfb3c7bf1208312f02a69e64bfd9e0.2791.D4ee7ff5d080dc--></protect>

==Notes==

==References==
{{RefHelp}}
<references/>


[[Category:Publication]]