1887

Abstract

Butane-grown ‘’ expressed two soluble alcohol dehydrogenases (ADHs), an NAD-dependent secondary ADH and an NAD-independent primary ADH. Two additional NAD-dependent secondary ADHs could be detected when cells were grown on 2-butanol and lactate. The inducible NAD-independent 1-butanol dehydrogenase (BDH) of butane-grown cells was primarily responsible for 1-butanol oxidation in the butane metabolism pathway. BDH was purified to near homogeneity and identified as a quinohaemoprotein, containing, per mol enzyme, 10 mol pyrroloquinoline quinone (PQQ) and 025 mol haem as prosthetic groups. BDH was synthesized as a monomer of approximately 66 kDa. It has a broad substrate range, including primary alcohols, secondary alcohols, aldehydes, C diols and aromatic alcohols. It exhibited the lowest (7±1 μM) and highest / (72×10 M s) value towards 1-butanol. BDH exhibited ferricyanide-dependent ADH activity. Calcium ions (up to 10 mM) increased BDH activity substantially. Two BDH internal amino acid sequences showed 73 and 62% identity and 83 and 66% similarity, respectively, when compared with an amino acid sequence of ethanol dehydrogenase from . The presence of the inducible BDH and secondary ADH may indicate that the terminal and subterminal oxidation pathways are involved in butane degradation of butane-grown ‘’.

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2001-03-01
2020-09-29
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