Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-11

AUTHORS

Raza Ashraf, Naeem Rashid, Tamotsu Kanai, Tadayuki Imanaka, Muhammad Akhtar

ABSTRACT

Genome sequence of Pyrobaculum calidifontis, a hyperthermophilic archaeon, harbors three open-reading frames annotated as alcohol dehydrogenases. One of them, Pcal_1311, does not display a significantly high homology with any of the characterized alcohol dehydrogenases. Highest homology of 38% was found with the characterized counterpart from Geobacillus stearothermophilus. To examine the biochemical properties of Pcal_1311, we have cloned and functionally expressed the gene in Escherichia coli. Purified recombinant Pcal_1311 catalyzed the NAD(H)-dependent oxidation of various alcohols and reduction of aldehydes, with a marked preference for substrates with functional group at the terminal carbon. Highest activity for the oxidation reaction (3 μmol min-1 mg-1) was found with 1,4-butanediol and for the reduction reaction (150 μmol min-1 mg-1) with glutaraldehyde. Both the oxidation and reduction activities increased with the increase in temperature up to 80 °C. Recombinant Pcal_1311 was highly stable and retained more than 90% activity even after incubation of 180 min at 90 °C. In addition to the thermostabilty, Pcal_1311 was highly stable in the presence of known denaturants including urea and guanidine hydrochloride. The high stability, particularly thermostability, and the NADH-dependent aldehyde reduction activity make Pcal_1311 a unique member in the alcohol dehydrogenase family. More... »

PAGES

1101-1110

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00792-017-0970-y

DOI

http://dx.doi.org/10.1007/s00792-017-0970-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1092151610

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29022135


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