Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541

Martin Karabec; Andrzej Lyskowski; Katharina C. Tauber; Georg Steinkellner; Wolfgang Kroutil; Gideon Grogan; Karl Gruber

doi:10.1039/c0cc00929f

Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541

Martin Karabec, Andrzej Lyskowski, Katharina C. Tauber, Georg Steinkellner, Wolfgang Kroutil, Gideon Grogan, Karl Gruber

Chemistry

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

Abstract

The structure of the alcohol dehydrogenase ADH-'A' from Rhodococcus ruber reveals possible reasons for its remarkable tolerance to organic co-solvents and suggests new directions for structure-informed mutagenesis to produce enzymes of altered substrate specificity or improved selectivity.

Original language	English
Pages (from-to)	6314-6316
Number of pages	3
Journal	Chemical Communications
Volume	46
Issue number	34
DOIs	https://doi.org/10.1039/c0cc00929f
Publication status	Published - 14 Sept 2010

Keywords

BIOCATALYTIC HYDROGEN-TRANSFER
SEC-ALCOHOLS
ENZYMATIC REDUCTION
CRYSTAL-STRUCTURE
CHIRAL ALCOHOLS
KETONES
OXIDATION
DSM-44541
ENZYMES

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abstract = "The structure of the alcohol dehydrogenase ADH-'A' from Rhodococcus ruber reveals possible reasons for its remarkable tolerance to organic co-solvents and suggests new directions for structure-informed mutagenesis to produce enzymes of altered substrate specificity or improved selectivity.",

keywords = "BIOCATALYTIC HYDROGEN-TRANSFER, SEC-ALCOHOLS, ENZYMATIC REDUCTION, CRYSTAL-STRUCTURE, CHIRAL ALCOHOLS, KETONES, OXIDATION, DSM-44541, ENZYMES",

author = "Martin Karabec and Andrzej Lyskowski and Tauber, {Katharina C.} and Georg Steinkellner and Wolfgang Kroutil and Gideon Grogan and Karl Gruber",

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doi = "10.1039/c0cc00929f",

language = "English",

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T1 - Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541

AU - Karabec, Martin

AU - Lyskowski, Andrzej

AU - Tauber, Katharina C.

AU - Steinkellner, Georg

AU - Kroutil, Wolfgang

AU - Grogan, Gideon

AU - Gruber, Karl

PY - 2010/9/14

Y1 - 2010/9/14

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AB - The structure of the alcohol dehydrogenase ADH-'A' from Rhodococcus ruber reveals possible reasons for its remarkable tolerance to organic co-solvents and suggests new directions for structure-informed mutagenesis to produce enzymes of altered substrate specificity or improved selectivity.

KW - BIOCATALYTIC HYDROGEN-TRANSFER

KW - SEC-ALCOHOLS

KW - ENZYMATIC REDUCTION

KW - CRYSTAL-STRUCTURE

KW - CHIRAL ALCOHOLS

KW - KETONES

KW - OXIDATION

KW - DSM-44541

KW - ENZYMES

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U2 - 10.1039/c0cc00929f

DO - 10.1039/c0cc00929f

M3 - Article

SN - 1359-7345

VL - 46

SP - 6314

EP - 6316

JO - Chemical Communications

JF - Chemical Communications

IS - 34

ER -

Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-'A' from Rhodococcus ruber DSM 44541

Abstract

Keywords

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