Document Detail

Purification and characterization of a cold-adapted isocitrate lyase and expression analysis of the cold-inducible isocitrate lyase gene from the psychrophilic bacterium Colwellia psychrerythraea.
MedLine Citation:
PMID:  12382116     Owner:  NLM     Status:  MEDLINE    
Isocitrate lyase (ICL) from Colwellia psychrerythraea, a psychrophilic bacterium, was purified and characterized. The subunit molecular mass was 64 kDa, which is larger than that of other bacterial ICLs. The optimal temperature for its activity was 25 degrees C, the value of K(m) for the substrate ( DL-isocitrate) was minimum at 15 degrees C, and the catalytic efficiency ( k(cat)/ K(m)) value was maximum at 20 degrees C. Furthermore, the enzyme was remarkably thermolabile and completely inactivated by incubation for 2 min at 30 degrees C. These features indicate that ICL from this bacterium is a typical cold-adapted enzyme. A partial amino acid sequence of the C. psychrerythraea ICL was very similar to that of the closely related psychrophile Colwellia maris. Expression of the gene encoding the C. psychrerythraea ICL was found to be induced by low temperatures and by acetate in the medium. The cold adaptation of the catalytic properties of ICL and the stimulated expression of its gene at low temperatures strongly suggest that this enzyme is important for the growth of this bacterium in a cold environment.
Seiya Watanabe; Naoto Yamaoka; Noriyuki Fukunaga; Yasuhiro Takada
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Publication Detail:
Type:  Journal Article     Date:  2002-05-23
Journal Detail:
Title:  Extremophiles : life under extreme conditions     Volume:  6     ISSN:  1431-0651     ISO Abbreviation:  Extremophiles     Publication Date:  2002 Oct 
Date Detail:
Created Date:  2002-10-16     Completed Date:  2003-03-18     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9706854     Medline TA:  Extremophiles     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  397-405     Citation Subset:  IM; S    
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita 10-jo Nishi 8-chome, Kita-ku, Sapporo 060-0810, Japan.
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MeSH Terms
Adaptation, Physiological*
Alteromonadaceae / enzymology*,  genetics,  physiology
Amino Acid Sequence
Bacterial Proteins / biosynthesis,  genetics*
Cations, Divalent / pharmacology
Cold Temperature*
Enzyme Induction
Gene Expression Regulation, Bacterial
Isocitrate Lyase / biosynthesis,  genetics*
Molecular Sequence Data
Protein Denaturation
Sequence Alignment
Sequence Homology, Amino Acid
Reg. No./Substance:
0/Bacterial Proteins; 0/Cations, Divalent; EC Lyase

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