Document Detail


Homologous Alkalophilic and Acidophilic L-Arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability.
MedLine Citation:
PMID:  23001647     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To study the pH dependence of l-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines the optimal pH (pH(opt)) for activity, whereas the N-terminal surface R residues play an important role in determining the pH(opt) for stability.
Authors:
Sang-Jae Lee; Sang Jun Lee; Yong-Jik Lee; Seong-Bo Kim; Sung-Kun Kim; Dong-Woo Lee
Related Documents :
24944747 - Discovery of novel imidazo[4,5-b]pyridines as potent and selective inhibitors of phosph...
24939097 - Recent advances in the discovery of zinc-binding motifs for the development of carbonic...
24527857 - A structural and energetic model for the slow-onset inhibition of the mycobacterium tub...
23184347 - Broad-substrate screen as a tool to identify substrates for bacterial gcn5-related n-ac...
11742007 - Identification of the active site of poly(a)-specific ribonuclease by site-directed mut...
22206487 - Design, synthesis, and biological evaluation of potent quinoline and pyrroloquinoline a...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-21
Journal Detail:
Title:  Applied and environmental microbiology     Volume:  78     ISSN:  1098-5336     ISO Abbreviation:  Appl. Environ. Microbiol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-19     Completed Date:  2013-04-22     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  7605801     Medline TA:  Appl Environ Microbiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8813-6     Citation Subset:  IM    
Affiliation:
Division of Applied Biology and Chemistry, Kyungpook National University, Daegu, South Korea. leehicam@knu.ac.kr
Data Bank Information
Bank Name/Acc. No.:
GENBANK/JQ945232;  JX218020
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aldose-Ketose Isomerases / chemistry,  genetics*,  metabolism*
Alicyclobacillus / enzymology,  genetics
Amino Acids / chemistry,  genetics,  metabolism
Catalytic Domain
DNA, Bacterial / chemistry,  genetics
DNA, Ribosomal / chemistry,  genetics
Hydrogen-Ion Concentration
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Stability*
RNA, Ribosomal, 16S / genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Amino Acids; 0/DNA, Bacterial; 0/DNA, Ribosomal; 0/RNA, Ribosomal, 16S; EC 5.3.1.-/Aldose-Ketose Isomerases; EC 5.3.1.4/L-arabinose isomerase
Comments/Corrections

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


Previous Document:  Heterotrophic archaea contribute to carbon cycling in low-pH, suboxic biofilm communities.
Next Document:  Anaerobic benzene oxidation by Geobacter species.