Structure of the branched‐chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction
Identifieur interne : 000566 ( Main/Exploration ); précédent : 000565; suivant : 000567Structure of the branched‐chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction
Auteurs : Catrine L. Berthold ; Dörte Gocke ; Martin D. Wood ; Finian J. Leeper ; Martina Pohl ; Gunter SchneiderSource :
- Acta Crystallographica Section D [ 1399-0047 ] ; 2007-12.
English descriptors
Abstract
The thiamin diphosphate (ThDP) dependent branched‐chain keto acid decarboxylase (KdcA) from Lactococcus lactis catalyzes the decarboxylation of 3‐methyl‐2‐oxobutanoic acid to 3‐methylpropanal (isobutyraldehyde) and CO2. The enzyme is also able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C—C bond formation, in particular for the enzymatic synthesis of diversely substituted 2‐hydroxyketones with high enantioselectivity. The crystal structures of recombinant holo‐KdcA and of a complex with an inhibitory ThDP analogue mimicking a reaction intermediate have been determined to resolutions of 1.6 and 1.8 Å, respectively. KdcA shows the fold and cofactor–protein interactions typical of thiamin‐dependent enzymes. In contrast to the tetrameric assembly displayed by most other ThDP‐dependent decarboxylases of known structure, KdcA is a homodimer. The crystal structures provide insights into the structural basis of substrate selectivity and stereoselectivity of the enzyme and thus are suitable as a framework for the redesign of the substrate profile in carboligation reactions.
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DOI: 10.1107/S0907444907050433
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure of the branched‐chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction</title><author><name sortKey="Berthold, Catrine L" sort="Berthold, Catrine L" uniqKey="Berthold C" first="Catrine L." last="Berthold">Catrine L. Berthold</name></author><author><name sortKey="Gocke, Dorte" sort="Gocke, Dorte" uniqKey="Gocke D" first="Dörte" last="Gocke">Dörte Gocke</name></author><author><name sortKey="Wood, Martin D" sort="Wood, Martin D" uniqKey="Wood M" first="Martin D." last="Wood">Martin D. Wood</name></author><author><name sortKey="Leeper, Finian J" sort="Leeper, Finian J" uniqKey="Leeper F" first="Finian J." last="Leeper">Finian J. Leeper</name></author><author><name sortKey="Pohl, Martina" sort="Pohl, Martina" uniqKey="Pohl M" first="Martina" last="Pohl">Martina Pohl</name></author><author><name sortKey="Schneider, Gunter" sort="Schneider, Gunter" uniqKey="Schneider G" first="Gunter" last="Schneider">Gunter Schneider</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:B6FD04F98A98592A24220E74396230C87C04639F</idno><date when="2007" year="2007">2007</date><idno type="doi">10.1107/S0907444907050433</idno><idno type="url">https://api.istex.fr/document/B6FD04F98A98592A24220E74396230C87C04639F/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000439</idno><idno type="wicri:Area/Main/Curation">000437</idno><idno type="wicri:Area/Main/Exploration">000566</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Exploration">000566</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Structure of the branched‐chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction</title><author><name sortKey="Berthold, Catrine L" sort="Berthold, Catrine L" uniqKey="Berthold C" first="Catrine L." last="Berthold">Catrine L. Berthold</name></author><author><name sortKey="Gocke, Dorte" sort="Gocke, Dorte" uniqKey="Gocke D" first="Dörte" last="Gocke">Dörte Gocke</name></author><author><name sortKey="Wood, Martin D" sort="Wood, Martin D" uniqKey="Wood M" first="Martin D." last="Wood">Martin D. Wood</name></author><author><name sortKey="Leeper, Finian J" sort="Leeper, Finian J" uniqKey="Leeper F" first="Finian J." last="Leeper">Finian J. Leeper</name></author><author><name sortKey="Pohl, Martina" sort="Pohl, Martina" uniqKey="Pohl M" first="Martina" last="Pohl">Martina Pohl</name></author><author><name sortKey="Schneider, Gunter" sort="Schneider, Gunter" uniqKey="Schneider G" first="Gunter" last="Schneider">Gunter Schneider</name></author></analytic><monogr></monogr><series><title level="j">Acta Crystallographica Section D</title><title level="j" type="abbrev">Acta Cryst. D</title><idno type="ISSN">1399-0047</idno><idno type="eISSN">1399-0047</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>5 Abbey Square, Chester, Cheshire CH1 2HU, England</pubPlace><date type="published" when="2007-12">2007-12</date><biblScope unit="volume">63</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="1217">1217</biblScope><biblScope unit="page" to="1224">1224</biblScope></imprint><idno type="ISSN">1399-0047</idno></series><idno type="istex">B6FD04F98A98592A24220E74396230C87C04639F</idno><idno type="DOI">10.1107/S0907444907050433</idno><idno type="ArticleID">AYDHV5093</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1399-0047</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>biocatalysis.</term><term>carboligation</term><term>stereoselectivity</term><term>thiamin diphosphate</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The thiamin diphosphate (ThDP) dependent branched‐chain keto acid decarboxylase (KdcA) from Lactococcus lactis catalyzes the decarboxylation of 3‐methyl‐2‐oxobutanoic acid to 3‐methylpropanal (isobutyraldehyde) and CO2. The enzyme is also able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C—C bond formation, in particular for the enzymatic synthesis of diversely substituted 2‐hydroxyketones with high enantioselectivity. The crystal structures of recombinant holo‐KdcA and of a complex with an inhibitory ThDP analogue mimicking a reaction intermediate have been determined to resolutions of 1.6 and 1.8 Å, respectively. KdcA shows the fold and cofactor–protein interactions typical of thiamin‐dependent enzymes. In contrast to the tetrameric assembly displayed by most other ThDP‐dependent decarboxylases of known structure, KdcA is a homodimer. The crystal structures provide insights into the structural basis of substrate selectivity and stereoselectivity of the enzyme and thus are suitable as a framework for the redesign of the substrate profile in carboligation reactions.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Berthold, Catrine L" sort="Berthold, Catrine L" uniqKey="Berthold C" first="Catrine L." last="Berthold">Catrine L. Berthold</name><name sortKey="Gocke, Dorte" sort="Gocke, Dorte" uniqKey="Gocke D" first="Dörte" last="Gocke">Dörte Gocke</name><name sortKey="Leeper, Finian J" sort="Leeper, Finian J" uniqKey="Leeper F" first="Finian J." last="Leeper">Finian J. Leeper</name><name sortKey="Pohl, Martina" sort="Pohl, Martina" uniqKey="Pohl M" first="Martina" last="Pohl">Martina Pohl</name><name sortKey="Schneider, Gunter" sort="Schneider, Gunter" uniqKey="Schneider G" first="Gunter" last="Schneider">Gunter Schneider</name><name sortKey="Wood, Martin D" sort="Wood, Martin D" uniqKey="Wood M" first="Martin D." last="Wood">Martin D. Wood</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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