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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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3-Hydroxyisobutyrate dehydrogenase, an impurity in commercial 3-hydroxybutyrate dehydrogenase.

The enzymic determination of D-3-hydroxybutyrate and acetoacetate normally involves the use of 3-hydroxybutyrate dehydrogenase (HBDH, EC 1.1.1.30) of bacterial origin. We show that HBDH from Rhodopseudomonas spheroides (BCL, grade II) contains a 3-hydroxyisobutyrate dehydrogenase (HIBDH) activity: activity with 3-hydroxyisobutyrate as substrate was greater than 10% of that with 3-hydroxybutyrate. However, HBDH could be prepared essentially free of HIBDH activity by incubation at 37 degrees C in the presence of 1 mM-CaCl2, to produce an enzyme preparation that may be used for the specific determination of 3-hydroxybutyrate. Use of the purified enzyme preparations indicated that a major product of valine metabolism in hemidiaphragms from 40 h-starved rats was 3-hydroxyisobutyrate rather than 3-hydroxybutyrate.[1]

References

  1. 3-Hydroxyisobutyrate dehydrogenase, an impurity in commercial 3-hydroxybutyrate dehydrogenase. Worrall, E.B., Gassain, S., Cox, D.J., Sugden, M.C., Palmer, T.N. Biochem. J. (1987) [Pubmed]
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