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Archives of Microbiology

, Volume 154, Issue 2, pp 179–186 | Cite as

Hydroaromatic metabolism in Rhodococcus rhodochrous: purification and characterisation of its NAD-dependent quinate dehydrogenase

  • Neil C. Bruce
  • Ronald B. Cain
Original Papers

Abstract

Quinate grown cells of Rhodococcus rhodochrous N75 metabolized both quinate and shikimate via protocatechuate to succinate and acetyl CoA. The initial enzyme of the hydroaromatic pathway, quinate dehydrogenase was purified 188-fold to electrophoretic homogeneity. The enzyme is a monomer with a native relative molecular mass of 44,000 and is NAD-dependent. The enzyme is highly stereospecific with regard to hydroaromatic substrates, oxidising only the axial hydroxyl group at C-3 of (-)-isomers of quinate, shikimate, dihydroshikimate and t-3,t-4-dihydroxycyclohexane-c-1-carboxylate, but shows activity with several NAD analogues.

Key words

Quinate dehydrogenase Rhodococcus rhodochrous Hydroaromatic dehydrogenase Quinate Shikimate Dehydroquinate Dehydroshikimate 

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Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • Neil C. Bruce
    • 1
  • Ronald B. Cain
    • 1
  1. 1.Environmental Microbiology Laboratory, Department of Agricultural and Environmental ScienceThe UniversityNewcastle upon TyneUK

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