1887

Abstract

Three alcohol dehydrogenases have been identified in sp. strain HO1-N: an NAD-dependent enzyme and two NADP-dependent enzymes. One of the NADP-dependent alcohol dehydrogenases was partially purified and was specific for long-chain substrates. With tetradecanol as substrate an apparent value of 5.2 μM was calculated. This enzyme has a pI of 4.5 and a molecular mass of 144 kDa. All three alcohol dehydrogenases were constitutively expressed. Three aldehyde dehydrogenases were also identified: an NAD-dependent enzyme, an NADP-dependent enzyme and one which was nucleotide independent. The NAD-dependent enzyme represented only 2% of the total activity and was not studied further. The NADP-dependent enzyme was strongly induced by growth of cells on alkanes and was associated with hydrocarbon vesicles. With tetradecanal as substrate an apparent value of 0.2 μM was calculated. The nucleotide-independent aldehyde dehydrogenase could use either Würster’s Blue or phenazine methosulphate (PMS) as an artificial electron acceptor. This enzyme represents approximately 80% of the total long-chain aldehyde oxidizing activity within the cell when the enzymes were induced by growing the cells on hexadecane. It is particulate but can be solubilized using Triton X-100. The enzyme has an apparent of 0.36 mM for decanal.

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1992-09-01
2021-05-13
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