A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool

Anastassja L. Akal; Ram Karan; Adrian Hohl; Intikhab Alam; Malvina M. Vogler; Stefan W. Grötzinger; Jörg Eppinger; Magnus Rueping

doi:10.1002/2211-5463.12557

A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool

Anastassja L. Akal, Ram Karan, Adrian Hohl, Intikhab Alam, Malvina M. Vogler, Stefan W. Grötzinger, Jörg Eppinger, Magnus Rueping

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Enzymes originating from hostile environments offer exceptional stability under industrial conditions and are therefore highly in demand. Using single-cell genome data, we identified the alcohol dehydrogenase gene, adh/a1a, from the Atlantis II Deep Red Sea brine pool. ADH/A1a is highly active at elevated temperatures and high salt concentrations (optima at 70 °C and 4 M KCl), and withstands organic solvents. The polyextremophilic ADH/A1a exhibits a broad substrate scope including aliphatic and aromatic alcohols and is able to reduce cinnamyl-methyl-ketone and raspberry ketone in the reverse reaction, making it a possible candidate for the production of chiral compounds. Here, we report the affiliation of ADH/A1a to a rare enzyme family of microbial cinnamyl-alcohol dehydrogenases and explain unique structural features for halo- and thermoadaptation.

Original language	English (US)
Pages (from-to)	194-205
Number of pages	12
Journal	FEBS Open Bio
Volume	9
Issue number	2
DOIs	https://doi.org/10.1002/2211-5463.12557
State	Published - Dec 18 2018

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10.1002/2211-5463.12557

https://repository.kaust.edu.sa/bitstream/10754/630173/1/Akal_et_al-2018-FEBS_Open_Bio.pdf

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title = "A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool",

abstract = "Enzymes originating from hostile environments offer exceptional stability under industrial conditions and are therefore highly in demand. Using single-cell genome data, we identified the alcohol dehydrogenase gene, adh/a1a, from the Atlantis II Deep Red Sea brine pool. ADH/A1a is highly active at elevated temperatures and high salt concentrations (optima at 70 °C and 4 M KCl), and withstands organic solvents. The polyextremophilic ADH/A1a exhibits a broad substrate scope including aliphatic and aromatic alcohols and is able to reduce cinnamyl-methyl-ketone and raspberry ketone in the reverse reaction, making it a possible candidate for the production of chiral compounds. Here, we report the affiliation of ADH/A1a to a rare enzyme family of microbial cinnamyl-alcohol dehydrogenases and explain unique structural features for halo- and thermoadaptation.",

author = "Akal, {Anastassja L.} and Ram Karan and Adrian Hohl and Intikhab Alam and Vogler, {Malvina M.} and Gr{\"o}tzinger, {Stefan W.} and J{\"o}rg Eppinger and Magnus Rueping",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: The research reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST). We thank Prof. Michael Groll for the support. We thank Jullian R. Vittenet for the support with the ICP-OES measurement.",

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doi = "10.1002/2211-5463.12557",

language = "English (US)",

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AU - Akal, Anastassja L.

AU - Karan, Ram

AU - Hohl, Adrian

AU - Alam, Intikhab

AU - Vogler, Malvina M.

AU - Grötzinger, Stefan W.

AU - Eppinger, Jörg

AU - Rueping, Magnus

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: The research reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST). We thank Prof. Michael Groll for the support. We thank Jullian R. Vittenet for the support with the ICP-OES measurement.

PY - 2018/12/18

Y1 - 2018/12/18

N2 - Enzymes originating from hostile environments offer exceptional stability under industrial conditions and are therefore highly in demand. Using single-cell genome data, we identified the alcohol dehydrogenase gene, adh/a1a, from the Atlantis II Deep Red Sea brine pool. ADH/A1a is highly active at elevated temperatures and high salt concentrations (optima at 70 °C and 4 M KCl), and withstands organic solvents. The polyextremophilic ADH/A1a exhibits a broad substrate scope including aliphatic and aromatic alcohols and is able to reduce cinnamyl-methyl-ketone and raspberry ketone in the reverse reaction, making it a possible candidate for the production of chiral compounds. Here, we report the affiliation of ADH/A1a to a rare enzyme family of microbial cinnamyl-alcohol dehydrogenases and explain unique structural features for halo- and thermoadaptation.

AB - Enzymes originating from hostile environments offer exceptional stability under industrial conditions and are therefore highly in demand. Using single-cell genome data, we identified the alcohol dehydrogenase gene, adh/a1a, from the Atlantis II Deep Red Sea brine pool. ADH/A1a is highly active at elevated temperatures and high salt concentrations (optima at 70 °C and 4 M KCl), and withstands organic solvents. The polyextremophilic ADH/A1a exhibits a broad substrate scope including aliphatic and aromatic alcohols and is able to reduce cinnamyl-methyl-ketone and raspberry ketone in the reverse reaction, making it a possible candidate for the production of chiral compounds. Here, we report the affiliation of ADH/A1a to a rare enzyme family of microbial cinnamyl-alcohol dehydrogenases and explain unique structural features for halo- and thermoadaptation.

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A polyextremophilic alcohol dehydrogenase from the Atlantis II Deep Red Sea brine pool

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