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dc.contributor.author
Zolghadr, Behnam
dc.contributor.author
Gasselhuber, Bernhard
dc.contributor.author
Windwarder, Markus
dc.contributor.author
Pabst, Martin
dc.contributor.author
Kracher, Daniel
dc.contributor.author
Kerndl, Martina
dc.contributor.author
Zayni, Sonja
dc.contributor.author
Hofinger-Horvath, Andreas
dc.contributor.author
Ludwig, Roland
dc.contributor.author
Haltrich, Dietmar
dc.contributor.author
Oostenbrink, Chris
dc.contributor.author
Obinger, Christian
dc.contributor.author
Kosma, Paul
dc.contributor.author
Messner, Paul
dc.contributor.author
Schäffer, Christina
dc.date.accessioned
2019-12-06T07:48:25Z
dc.date.available
2017-06-11T16:08:23Z
dc.date.available
2019-12-06T07:48:25Z
dc.date.issued
2015-03
dc.identifier.other
10.1007/s00792-015-0730-9
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/98106
dc.identifier.doi
10.3929/ethz-b-000098106
dc.description.abstract
The UDP-sulfoquinovose synthase Agl3 from Sulfolobus acidocaldarius converts UDP-d-glucose and sulfite to UDP-sulfoquinovose, the activated form of sulfoquinovose required for its incorporation into glycoconjugates. Based on the amino acid sequence, Agl3 belongs to the short-chain dehydrogenase/reductase enzyme superfamily, together with SQD1 from Arabidopsis thaliana, the only UDP-sulfoquinovose synthase with known crystal structure. By comparison of sequence and structure of Agl3 and SQD1, putative catalytic amino acids of Agl3 were selected for mutational analysis. The obtained data suggest for Agl3 a modified dehydratase reaction mechanism. We propose that in vitro biosynthesis of UDP-sulfoquinovose occurs through an NAD+-dependent oxidation/dehydration/enolization/sulfite addition process. In the absence of a sulfur donor, UDP-d-glucose is converted via UDP-4-keto-d-glucose to UDP-d-glucose-5,6-ene, the structure of which was determined by 1H and 13C-NMR spectroscopy. During the redox reaction the cofactor remains tightly bound to Agl3 and participates in the reaction in a concentration-dependent manner. For the first time, the rapid initial electron transfer between UDP-d-glucose and NAD+ could be monitored in a UDP-sulfoquinovose synthase. Deuterium labeling confirmed that dehydration of UDP-d-glucose occurs only from the enol form of UDP-4-keto-glucose. The obtained functional data are compared with those from other UDP-sulfoquinovose synthases. A divergent evolution of Agl3 from S. acidocaldarius is suggested.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Springer
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
UDP-sulfoquinovose synthase Agl3
en_US
dc.subject
Sulfolobus acidocaldarius
en_US
dc.subject
Enzyme mechanism
en_US
dc.subject
Site-directed mutagenesis
en_US
dc.subject
Sulfite
en_US
dc.title
UDP-sulfoquinovose formation by Sulfolobus acidocaldarius
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2015-01-21
ethz.journal.title
Extremophiles
ethz.journal.volume
19
en_US
ethz.journal.issue
2
en_US
ethz.pages.start
451
en_US
ethz.pages.end
467
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.scopus
ethz.identifier.nebis
001753809
ethz.publication.place
Tokyo
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2017-06-11T16:08:51Z
ethz.source
ECIT
ethz.identifier.importid
imp593652ed7f3d738644
ethz.ecitpid
pub:153406
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-17T09:31:36Z
ethz.rosetta.lastUpdated
2019-12-06T07:48:40Z
ethz.rosetta.versionExported
true
ethz.COinS
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