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Characterization of a Thermoacidophilic l-Arabinose Isomerase from Alicyclobacillus acidocaldarius: Role of Lys-269 in pH Optimum

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Published in:Applied and Environmental Microbiology 2005-12, Vol.71 (12), p.7888-7896
Main Authors: LEE, Sang-Jae, LEE, Dong-Woo, CHOC, Eun-Ah, HONG, Young-Ho, KIM, Seong-Bo, KIM, Byoung-Chan, PYUN, Yu-Ryang
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description Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue AEM About AEM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AEM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0099-2240 Online ISSN: 1098-5336 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to AEM .asm.org, visit: AEM       
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source PubMed Central (Open Access); American Society for Microbiology
subjects Aldose-Ketose Isomerases - chemistry
Aldose-Ketose Isomerases - genetics
Aldose-Ketose Isomerases - metabolism
Alicyclobacillus acidocaldarius
Amino Acid Sequence
Bacillus halodurans
Bacteria
Base Sequence
Biological and medical sciences
Biotechnology
DNA Primers
Enzymes
Enzymology and Protein Engineering
Escherichia coli
Fundamental and applied biological sciences. Psychology
Genes
Geobacillus stearothermophilus
Gram-Positive Endospore-Forming Rods - enzymology
Gram-Positive Endospore-Forming Rods - genetics
Hydrogen-Ion Concentration
Kinetics
Lysine
Microbiology
Molecular Sequence Data
Mutagenesis, Site-Directed
Polymerase Chain Reaction
Protein Structure, Secondary
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Thermodynamics
title Characterization of a Thermoacidophilic l-Arabinose Isomerase from Alicyclobacillus acidocaldarius: Role of Lys-269 in pH Optimum
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