Electrostatic stabilization in alcohol dehydrogenase mechanisms: the oxyanion hole of D-mannitol 2-dehydrogenase from Pseudomonas fluorescens is a novel structural motif that facilitates the catalytic step of hydride transfer

Research output: Contribution to conferencePosterResearch

Original languageEnglish
Publication statusPublished - 2006
EventEnzymology and molecular biology of carbonyl metabolism - Nashville, Indiana
Duration: 11 Jul 200612 Jul 2006

Conference

ConferenceEnzymology and molecular biology of carbonyl metabolism
CityNashville, Indiana
Period11/07/0612/07/06

Treatment code (Nähere Zuordnung)

  • Basic - Fundamental (Grundlagenforschung)

Cite this

Electrostatic stabilization in alcohol dehydrogenase mechanisms: the oxyanion hole of D-mannitol 2-dehydrogenase from Pseudomonas fluorescens is a novel structural motif that facilitates the catalytic step of hydride transfer. / Klimacek, Mario; Nidetzky, Bernd.

2006. Poster session presented at Enzymology and molecular biology of carbonyl metabolism, Nashville, Indiana, .

Research output: Contribution to conferencePosterResearch

@conference{fcbed37dd4554816ac44805ca3e78e69,
title = "Electrostatic stabilization in alcohol dehydrogenase mechanisms: the oxyanion hole of D-mannitol 2-dehydrogenase from Pseudomonas fluorescens is a novel structural motif that facilitates the catalytic step of hydride transfer",
author = "Mario Klimacek and Bernd Nidetzky",
year = "2006",
language = "English",
note = "Enzymology and molecular biology of carbonyl metabolism ; Conference date: 11-07-2006 Through 12-07-2006",

}

TY - CONF

T1 - Electrostatic stabilization in alcohol dehydrogenase mechanisms: the oxyanion hole of D-mannitol 2-dehydrogenase from Pseudomonas fluorescens is a novel structural motif that facilitates the catalytic step of hydride transfer

AU - Klimacek, Mario

AU - Nidetzky, Bernd

PY - 2006

Y1 - 2006

M3 - Poster

ER -