Characterization of NADP+-dependent isocitrate dehydrogenase isozymes from a psychrophilic bacterium, Colwellia psychrerythraea strain 34H
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چکیده
منابع مشابه
Motility of Colwellia psychrerythraea strain 34H at subzero temperatures.
We examined the Arctic bacterium Colwellia psychrerythraea strain 34H for motility at temperatures from -1 to -15 degrees C by using transmitted-light microscopy in a temperature-controlled laboratory. The results, showing motility to -10 degrees C, indicate much lower temperatures to be permissive of motility than previously reported (5 degrees C), with implications for microbial activity in f...
متن کاملA unique capsular polysaccharide structure from the psychrophilic marine bacterium Colwellia psychrerythraea 34H that mimics antifreeze (glyco)proteins.
The low temperatures of polar regions and high-altitude environments, especially icy habitats, present challenges for many microorganisms. Their ability to live under subfreezing conditions implies the production of compounds conferring cryotolerance. Colwellia psychrerythraea 34H, a γ-proteobacterium isolated from subzero Arctic marine sediments, provides a model for the study of life in cold ...
متن کاملCrystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H
Isoaspartyl dipeptidase (IadA) is an enzyme that catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the β-carboxyl group side chain of Asp and the amino group of the following amino acid. Here, we have determined the structures of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea, both ligand-free and that...
متن کاملAnalysis of amino acid residues involved in cold activity of monomeric isocitrate dehydrogenase from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea.
Monomeric isocitrate dehydrogenases from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea (CmIDH-II and CpIDH-M, respectively) are cold-adapted enzymes and show a high degree of amino acid sequential identity to each other (77%). However, maximum activity of CpIDH-M at optimum temperature is much less than that of CmIDH-II. In the C-terminal region 3 of these enzymes, which...
متن کاملAmino acid residues involved in cold adaptation of isocitrate lyase from a psychrophilic bacterium, Colwellia maris.
To investigate the mechanism of cold adaptation of isocitrate lyase (ICL; EC 4.1.3.1) from the psychrophilic bacterium Colwellia maris, Gln207 and Gln217 of this enzyme were substituted by His and Lys, respectively, by site-directed mutagenesis. His184 and Lys194 of ICL from Escherichia coli, corresponding to the two Gln residues of C. maris ICL, are highly conserved in the ICLs of many organis...
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ژورنال
عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry
سال: 2016
ISSN: 0916-8451,1347-6947
DOI: 10.1080/09168451.2016.1165602