4bt2: Difference between revisions
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==acetolactate decarboxylase with a bound 1,2-ETHANEDIOL== | |||
=== | <StructureSection load='4bt2' size='340' side='right' caption='[[4bt2]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bt2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BT2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bt3|4bt3]], [[4bt4|4bt4]], [[4bt5|4bt5]], [[4bt6|4bt6]], [[4bt7|4bt7]]</td></tr> | |||
<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> | |||
<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=4bt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bt2 RCSB], [http://www.ebi.ac.uk/pdbsum/4bt2 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetolactate decarboxylase]] | [[Category: Acetolactate decarboxylase]] | ||
[[Category: Brevibacillus brevis]] | [[Category: Brevibacillus brevis]] | ||
[[Category: Fulop, V | [[Category: Fulop, V]] | ||
[[Category: Marlow, V A | [[Category: Marlow, V A]] | ||
[[Category: Najmudin, S | [[Category: Najmudin, S]] | ||
[[Category: Rea, D | [[Category: Rea, D]] | ||
[[Category: Wills, M | [[Category: Wills, M]] | ||
[[Category: Acetoin biosynthesis]] | [[Category: Acetoin biosynthesis]] | ||
[[Category: Bifunctional enzyme]] | [[Category: Bifunctional enzyme]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Stereoselective decarboxylation]] | [[Category: Stereoselective decarboxylation]] | ||
