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

Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity
Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity
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.
1431-0651
1101-1110
Ashraf, Raza
8fc49418-8f6d-4b7a-bcd5-78ea8636fd5a
Rashid, Naeem
81704b5b-8999-4883-8e58-0c09ab9b63e1
Kanai, Tamotsu
1bd70a1d-7cbb-40b4-83c8-854c2333a658
Imanaka, Tadayuki
b1a443e1-5ff3-4e46-84ff-a8be5c27d074
Akhtar, Muhammad
a4174002-a6bd-4678-8e63-4cbe607a672d
Ashraf, Raza
8fc49418-8f6d-4b7a-bcd5-78ea8636fd5a
Rashid, Naeem
81704b5b-8999-4883-8e58-0c09ab9b63e1
Kanai, Tamotsu
1bd70a1d-7cbb-40b4-83c8-854c2333a658
Imanaka, Tadayuki
b1a443e1-5ff3-4e46-84ff-a8be5c27d074
Akhtar, Muhammad
a4174002-a6bd-4678-8e63-4cbe607a672d

Ashraf, Raza, Rashid, Naeem, Kanai, Tamotsu, Imanaka, Tadayuki and Akhtar, Muhammad (2017) Pcal_1311, an alcohol dehydrogenase homologue from Pyrobaculum calidifontis, displays NADH-dependent high aldehyde reductase activity. Extremophiles, 1101-1110. (doi:10.1007/s00792-017-0970-y).

Record type: Article

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.

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More information

Accepted/In Press date: 25 September 2017
e-pub ahead of print date: 11 October 2017
Published date: November 2017

Identifiers

Local EPrints ID: 418228
URI: https://eprints.soton.ac.uk/id/eprint/418228
ISSN: 1431-0651
PURE UUID: 4edcd0d0-f607-44c0-b684-dc9489f9719d

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Date deposited: 23 Feb 2018 17:31
Last modified: 13 Mar 2019 19:17

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Contributors

Author: Raza Ashraf
Author: Naeem Rashid
Author: Tamotsu Kanai
Author: Tadayuki Imanaka
Author: Muhammad Akhtar

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