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| | ==P. putida mandelate racemase in complex with 3-hydroxypyruvate== | | ==P. putida mandelate racemase in complex with 3-hydroxypyruvate== |
| - | <StructureSection load='4x2p' size='340' side='right' caption='[[4x2p]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='4x2p' size='340' side='right'caption='[[4x2p]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4x2p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X2P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4x2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X2P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdlA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2p OCA], [https://pdbe.org/4x2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x2p RCSB], [https://www.ebi.ac.uk/pdbsum/4x2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x2p ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mandelate_racemase Mandelate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.2.2 5.1.2.2] </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=4x2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x2p OCA], [http://pdbe.org/4x2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x2p RCSB], [http://www.ebi.ac.uk/pdbsum/4x2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x2p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MANR_PSEPU MANR_PSEPU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4x2p" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4x2p" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Mandelate racemase|Mandelate racemase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens putidus flugge 1886]] | + | [[Category: Large Structures]] |
| - | [[Category: Mandelate racemase]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: St Maurice, M]] | + | [[Category: StMaurice M]] |
| - | [[Category: Wyatt, B N]] | + | [[Category: Wyatt BN]] |
| - | [[Category: Enolase superfamily]]
| + | |
| - | [[Category: Isomerase]]
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| - | [[Category: Racemase]]
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| Structural highlights
Function
MANR_PSEPU
Publication Abstract from PubMed
Mandelate racemase (MR), a member of the enolase superfamily, catalyzes the Mg(2+)-dependent interconversion of the enantiomers of mandelate. Several alpha-keto acids are modest competitive inhibitors of MR [e.g., mesoxalate (Ki = 1.8 +/- 0.3 mM) and 3-fluoropyruvate (Ki = 1.3 +/- 0.1 mM)], but, surprisingly, 3-hydroxypyruvate (3-HP) is an irreversible, time-dependent inhibitor (kinact/KI = 83 +/- 8 M(-1) s(-1)). Protection from inactivation by the competitive inhibitor benzohydroxamate, trypsinolysis and electrospray ionization tandem mass spectrometry analyses, and X-ray crystallographic studies reveal that 3-HP undergoes Schiff-base formation with Lys 166 at the active site, followed by formation of an aldehyde/enol(ate) adduct. Such a reaction is unprecedented in the enolase superfamily and may be a relic of an activity possessed by a promiscuous progenitor enzyme. The ability of MR to form and deprotonate a Schiff-base intermediate furnishes a previously unrecognized mechanistic link to other alpha/beta-barrel enzymes utilizing Schiff-base chemistry and is in accord with the sequence- and structure-based hypothesis that members of the metal-dependent enolase superfamily and the Schiff-base-forming N-acetylneuraminate lyase superfamily and aldolases share a common ancestor.
Inactivation of Mandelate Racemase by 3-Hydroxypyruvate Reveals a Potential Mechanistic Link between Enzyme Superfamilies.,Nagar M, Wyatt BN, St Maurice M, Bearne SL Biochemistry. 2015 May 5;54(17):2747-57. doi: 10.1021/acs.biochem.5b00221. Epub, 2015 Apr 20. PMID:25844917[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nagar M, Wyatt BN, St Maurice M, Bearne SL. Inactivation of Mandelate Racemase by 3-Hydroxypyruvate Reveals a Potential Mechanistic Link between Enzyme Superfamilies. Biochemistry. 2015 May 5;54(17):2747-57. doi: 10.1021/acs.biochem.5b00221. Epub, 2015 Apr 20. PMID:25844917 doi:http://dx.doi.org/10.1021/acs.biochem.5b00221
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