4rjk: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rjk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rjk RCSB], [http://www.ebi.ac.uk/pdbsum/4rjk PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rjk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rjk RCSB], [http://www.ebi.ac.uk/pdbsum/4rjk PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Isobutanol is deemed to be a next-generation biofuel and a renewable platform chemical.1 Non-natural biosynthetic pathways for isobutanol production have been implemented in cell-based and in vitro systems with Bacillus subtilis acetolactate synthase (AlsS) as key biocatalyst.2-6 AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. AlsS also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol. Our phylogenetic analysis suggests that the ALS enzyme family forms a distinct subgroup of ThDP-dependent enzymes. To unravel catalytically relevant structure-function relationships, we solved the AlsS crystal structure at 2.3 A in the presence of ThDP, Mg2+ and in a transition state with a 2-lactyl moiety bound to ThDP. We supplemented our structural data by point mutations in the active site to identify catalytically important residues. | |||
Detailed Structure-Function Correlations of Bacillus subtilis Acetolactate Synthase.,Sommer B, von Moeller H, Haack M, Qoura F, Langner C, Bourenkov G, Garbe D, Loll B, Bruck T Chembiochem. 2014 Nov 13. doi: 10.1002/cbic.201402541. PMID:25393087<ref>PMID:25393087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Bourenkov, G | [[Category: Bourenkov, G]] | ||
[[Category: Brueck, T | [[Category: Brueck, T]] | ||
[[Category: Garbe, D | [[Category: Garbe, D]] | ||
[[Category: Haack, M | [[Category: Haack, M]] | ||
[[Category: Langner, C | [[Category: Langner, C]] | ||
[[Category: Loll, B | [[Category: Loll, B]] | ||
[[Category: Moeller, H von | [[Category: Moeller, H von]] | ||
[[Category: Qoura, F | [[Category: Qoura, F]] | ||
[[Category: Sommer, B | [[Category: Sommer, B]] | ||
[[Category: Thdp]] | [[Category: Thdp]] | ||