Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N‐terminal sequence

The isocitrate dehydrogenases from the extremely halophilic Archaeon, Haloferax uolcanii, and from the hyperthermophilic Archaeon, Sulfolobus solfataricus, have been purified to electrophoretic homogeneity. The purified enzymes have been characterised with respect to their cofactor specificities, su...

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Bibliographic Details
Published in:FEMS microbiology letters 1995-12, Vol.134 (1), p.85-90
Main Authors: Camacho, Mónica L., Brown, Richard A., Bonete, María‐josé, Danson, Michael J., Hough, David W.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Archaea
Bacteriology
Biological and medical sciences
Catalysis - drug effects
Enzyme Stability
Fundamental and applied biological sciences. Psychology
Halobacteriaceae - enzymology
Haloferax volcanii
Halophile
Hot Temperature
Isocitrate dehydrogenase
Isocitrate Dehydrogenase - chemistry
Isocitrate Dehydrogenase - genetics
Isocitrate Dehydrogenase - isolation & purification
Isocitrate Dehydrogenase - metabolism
Kinetics
Metabolism. Enzymes
Microbiology
Molecular Sequence Data
Molecular Weight
Potassium Chloride - pharmacology
Purification
Sequence Alignment
Sequence Analysis
Stability
Sulfolobus - enzymology
Sulfolobus solfataricus
Thermophile
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Summary:The isocitrate dehydrogenases from the extremely halophilic Archaeon, Haloferax uolcanii, and from the hyperthermophilic Archaeon, Sulfolobus solfataricus, have been purified to electrophoretic homogeneity. The purified enzymes have been characterised with respect to their cofactor specificities, subunit compositions and their salt and thermal stabilities. N‐terminal amino acid sequences have been determined for both enzymes, and multiple alignments with sequences of bacterial and eukaryotic isocitrate dehydrogenases show that the archaeal enzymes most closely resemble the NADP‐linked dimeric isocitrate dehydrogenases from the Bacteria.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1995.tb07919.x