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Eur J Biochem. 1987 Sep 15;167(3):475-9.

A novel archaebacterial NAD+-dependent alcohol dehydrogenase. Purification and properties.

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1
Istituto Internazionale di Genetica e Biofisica, Consiglio Nazionale delle Richerche, Napoli, Italy.

Abstract

An NAD+-dependent alcohol dehydrogenase (alcohol: NAD+ oxidoreductase, EC 1.1.1.1) was detected in cellular extracts of the extreme thermophilic archaebacterium Sulfolobus solfataricus. The enzyme was purified to homogeneity and shown to be a dimer with a native molecular mass of 71 kDa by sucrose gradient centrifugation and SDS electrophoresis. The enzyme has a broad substrate specificity that includes linear and branched primary alcohols, linear and cyclic secondary alcohols, linear and cyclic ketones and anisaldehyde. The enzyme has an extraordinary thermophilicity and a remarkable thermostability, and appears to have some properties and a structure different from those previously described for thermophilic alcohol dehydrogenases.

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