Document Detail


Characterization of a recombinant L-fucose isomerase from Caldicellulosiruptor saccharolyticus that isomerizes L-fucose, D-arabinose, D-altrose, and L-galactose.
MedLine Citation:
PMID:  19856146     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A recombinant L-fucose isomerase from Caldicellulosiruptor saccharolyticus was purified as a single 68 kDa band with an activity of 76 U mg(-1). The molecular mass of the native enzyme was 204 kDa as a trimer. The maximum activity for L-fucose isomerization was at pH 7 and 75 degrees C in the presence of 1 mM Mn(2+). Its half-life at 70 degrees C was 6.1 h. For aldose substrates, the enzyme displayed activity in decreasing order for L-fucose, with a k (cat) of 11,910 min(-1) and a K (m) of 140 mM, D-arabinose, D-altrose, and L-galactose. These aldoses were converted to the ketoses L-fuculose, D-ribulose, D-psicose, and L-tagatose, respectively, with 24, 24, 85, 55% conversion yields after 3 h.
Authors:
Yo-Han Ju; Deok-Kun Oh
Related Documents :
21612976 - Novel metabolic pathways in archaea.
12916726 - Purification and some properties of exo-1,4-beta-glucanase from chaetomium olivaceum.
10206696 - Partial characterization of a major autolysin from mycobacterium phlei.
3026366 - [phosphotyrosine]protein phosphatase in rat brain. a major [phosphotyrosine]protein pho...
3559266 - Retinol esterification by mouse epidermal microsomes: evidence for acyl-coa:retinol acy...
3008716 - Amino acid sequence homology among fructose-1,6-bisphosphatases.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-10-25
Journal Detail:
Title:  Biotechnology letters     Volume:  32     ISSN:  1573-6776     ISO Abbreviation:  Biotechnol. Lett.     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-01-21     Completed Date:  2010-03-02     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  299-304     Citation Subset:  IM    
Affiliation:
Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, South Korea.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aldose-Ketose Isomerases / chemistry*,  genetics,  metabolism*
Arabinose / chemistry*
Enzyme Activation
Fucose / chemistry*
Galactose / chemistry*
Isomerism
Recombinant Proteins / chemistry*,  metabolism
Thermoanaerobacterium / enzymology*,  genetics
Chemical
Reg. No./Substance:
0/Recombinant Proteins; 147-81-9/Arabinose; 26566-61-0/Galactose; 3713-31-3/Fucose; EC 5.3.1/Aldose-Ketose Isomerases; EC 5.3.1.3/D-arabinose isomerase

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


Previous Document:  Phospholipase D modulation by ceramide in senescence.
Next Document:  Inhibitory effect of curcumin on liver injury in a murine model of endotoxemic shock.