Characterization of NADP(+)-dependent isocitrate dehydrogenase isozymes from a psychrophilic bacterium, Colwellia psychrerythraea strain 34H

Bioscience, Biotechnology, and Biochemistry
Kaori Suzuki, Yasuhiro Takada

Abstract

NADP(+)-dependent isocitrate dehydrogenase (IDH) isozymes of a psychrophilic bacterium, Colwellia psychrerythraea strain 34H, were characterized. The coexistence of monomeric and homodimeric IDHs in this bacterium was confirmed by Western blot analysis, the genes encoding two monomeric (IDH-IIa and IDH-IIb) and one dimeric (IDH-I) IDHs were cloned and overexpressed in Escherichia coli, and the three IDH proteins were purified. Both of the purified IDH-IIa and IDH-IIb were found to be cold-adapted enzymes while the purified IDH-I showed mesophilic properties. However, the specific activities of IDH-IIa and IDH-IIb were lower even at low temperatures than that of IDH-I. Therefore, IDH-I was suggested to be important for the growth of this bacterium. The results of colony formation of E. coli transformants carrying the respective IDH genes and IDH activities in their crude extracts indicated that the expression of the IDH-IIa gene is cold-inducible in the E. coli cells.

References

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Nov 1, 1972·Archives of Biochemistry and Biophysics·A E Chung, J E Braginski
Sep 1, 1974·Journal of Bacteriology·F C NeidhardtD F Smith
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Mar 10, 2001·Environmental Microbiology·Adrienne L HustonJody W Deming
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Jan 19, 2006·Extremophiles : Life Under Extreme Conditions·Shinsuke MakiYasuhiro Takada
Jun 16, 2010·Archives of Microbiology·Shougo MatsuoYasuhiro Takada

Methods Mentioned

BETA
PCR
column chromatography

Related Concepts

Idp1 protein, S pombe
Adaptation, Physiological
Bacterial Proteins
Chromosomes, Bacterial
Cold Temperature
Enzyme Stability
Alkalescens-Dispar Group
Isocitrate Dehydrogenase-I
Alloenzymes
Episomes

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