Characterization of two 3-hydroxybutyrate dehydrogenases in poly(3-hydroxybutyrate)-degradable bacterium, Ralstonia pickettii T1

Journal of Bioscience and Bioengineering
Masahiko Takanashi, T Saito

Abstract

Two D-(-)-3-hydroxybutyrate (3HB) dehydrogenases, BDH1 and BDH2, were isolated and purified from a poly(3-hydroxybutyrate) (PHB)-degradable bacterium, Ralstonia pickettii T1. BDH1 activity increased in R. pickettii T1 cells grown on several organic acids as a carbon source but not on 3HB, whereas BDH2 activity markedly increased in the same cells grown on 3HB or PHB. To examine their biochemical properties, bdh1 and bdh2 were cloned and overexpressed in Escherichia coli, and their purified products were characterized. The kinetic parameters indicate that BDH1 is more suitable for converting acetoacetate to 3HB than BDH2, whereas BDH2 is more efficient for the reverse reaction than BDH1. Thus, R. pickettii T1 contains two BDHs with different biochemical properties and physiological roles: BDH1 for cell growth on organic acids other than 3HB and BDH2 for cell growth on 3HB or PHB.

References

Sep 1, 1991·European Journal of Biochemistry·B PerssonH Jörnvall
Oct 5, 1990·Journal of Molecular Biology·S F AltschulD J Lipman
Jul 1, 1968·Canadian Journal of Microbiology·P JurtshukC R Barrera
Aug 1, 1969·Journal of General Microbiology·P F Fottrell, A O'Hora
Oct 20, 2005·Journal of Bioscience and Bioengineering·Masahiko TakanashiTerumi Saito

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Citations

Sep 18, 2008·Toxicological Sciences : an Official Journal of the Society of Toxicology·Mary B DailShane C Burgess
Feb 17, 2009·Antonie van Leeuwenhoek·Masahiko TakanashiTerumi Saito
Mar 14, 2008·The Journal of Microbiology·Eun Young LeeKeun Kim
Mar 15, 2008·Antonie van Leeuwenhoek·Akiko SugimotoTerumi Saito

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