4bt6

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<StructureSection load='4bt6' size='340' side='right'caption='[[4bt6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4bt6' size='340' side='right'caption='[[4bt6]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bt6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BT6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BT6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bt2|4bt2]], [[4bt3|4bt3]], [[4bt4|4bt4]], [[4bt5|4bt5]], [[4bt7|4bt7]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt6 OCA], [https://pdbe.org/4bt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bt6 RCSB], [https://www.ebi.ac.uk/pdbsum/4bt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt6 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetolactate_decarboxylase Acetolactate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.5 4.1.1.5] </span></td></tr>
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<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=4bt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt6 OCA], [http://pdbe.org/4bt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bt6 RCSB], [http://www.ebi.ac.uk/pdbsum/4bt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt6 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/ALDC_BREBE ALDC_BREBE]]
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Acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that has been shown to involve a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer. In this paper, a series of crystal structures of ALDC complex with designed transition state mimics are reported. These structures, coupled with inhibition studies and site-directed mutagenesis provide an improved understanding of the molecular processes involved in the stereoselective decarboxylation/protonation events. A mechanism for the transformation of each enantiomer of acetolactate is proposed.
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Structure and Mechanism of Acetolactate Decarboxylase.,Marlow VA, Rea D, Najmudin S, Wills M, Fulop V ACS Chem Biol. 2013 Aug 28. PMID:23985082<ref>PMID:23985082</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4bt6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetolactate decarboxylase]]
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[[Category: Brevibacillus brevis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fulop, V]]
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[[Category: A Marlow V]]
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[[Category: Marlow, V A]]
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[[Category: Fulop V]]
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[[Category: Najmudin, S]]
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[[Category: Najmudin S]]
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[[Category: Rea, D]]
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[[Category: Rea D]]
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[[Category: Wills, M]]
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[[Category: Wills M]]
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[[Category: Acetoin biosynthesis]]
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[[Category: Bifunctional enzyme]]
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[[Category: Lyase]]
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[[Category: Stereoselective decarboxylation]]
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Revision as of 17:06, 7 September 2022

acetolactate decarboxylase with a bound glycerol

PDB ID 4bt6

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