Document Detail


Characterization of a recombinant thermostable dehalogenase isolated from the hot spring thermophile Sulfolobus tokodaii.
MedLine Citation:
PMID:  19266316     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A putative dehalogenase, L-HAD(ST), from the thermophile Sulfolobus tokodaii, was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzes the stereospecific dehalogenation of L-2-haloacids with similar levels of activity as its homolog from mesophiles. L-HAD(ST) remains fully active after being incubated for 4 h at 70 degrees C and tolerates extreme pH conditions ranging from 4 to 10. Furthermore, it can be purified conveniently without the usage of any chromatography method. The high expression yield and easy purification procedure make the recombinant dehalogenase an excellent candidate for biotechnological applications.
Authors:
Philip G Bachas-Daunert; Stacy A Law; Yinan Wei
Related Documents :
8365406 - High expression in escherichia coli of the gene coding for dihydrofolate reductase of t...
11526206 - In vivo mechanism-based inactivation of s-adenosylmethionine decarboxylases from escher...
16023116 - Identification of escherichia coli k12 ydcw protein as a gamma-aminobutyraldehyde dehyd...
18710396 - Cloning and sequencing of the gene for cellobiose 2-epimerase from a ruminal strain of ...
12921536 - The unique features of glycolytic pathways in archaea.
9459016 - Anti-plasmodial and anti-trypanosomal activity of synthetic naphtho[2,3-b]thiopen-4,9-q...
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2009-03-06
Journal Detail:
Title:  Applied biochemistry and biotechnology     Volume:  159     ISSN:  1559-0291     ISO Abbreviation:  Appl. Biochem. Biotechnol.     Publication Date:  2009 Nov 
Date Detail:
Created Date:  2009-10-05     Completed Date:  2009-12-09     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8208561     Medline TA:  Appl Biochem Biotechnol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  382-93     Citation Subset:  IM    
Affiliation:
Paul Laurence Dunbar High School, Lexington, KY 40513, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Cloning, Molecular / methods*
Enzyme Activation
Enzyme Stability
Escherichia coli / physiology
Hot Springs / microbiology*
Hydrolases / chemistry*,  genetics,  metabolism*
Protein Engineering / methods*
Recombinant Proteins / chemistry,  isolation & purification,  metabolism
Sulfolobus / enzymology*,  genetics,  metabolism*
Temperature
Grant Support
ID/Acronym/Agency:
P42 ES07380/ES/NIEHS NIH HHS
Chemical
Reg. No./Substance:
0/Recombinant Proteins; EC 3.-/Hydrolases; EC 3.8.1.2/2-haloacid dehalogenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Trial by CCN2: a standardized test for fibroproliferative disease?
Next Document:  Exploring the Role of C-H....pi Interactions on the Structural Stability of Single Chain "All-Alpha"...