2yii: Difference between revisions

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'''Unreleased structure'''


The entry 2yii is ON HOLD
==Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution==
<StructureSection load='2yii' size='340' side='right'caption='[[2yii]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yii]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Taxus_chinensis Taxus chinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YII FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene></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=2yii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yii OCA], [https://pdbe.org/2yii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yii RCSB], [https://www.ebi.ac.uk/pdbsum/2yii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yii ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAM_TAXWC PAM_TAXWC] Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first commited step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.<ref>PMID:15878763</ref> <ref>PMID:22113970</ref> <ref>PMID:24786474</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regioselective amination of cinnamate derivatives (see scheme, red) to, for example, beta-amino acids. This regioselectivity, along with the X-ray crystal structures, suggests two distinct carboxylate binding modes differentiated by C(beta)-C(ipso) bond rotation, which determines if beta- (see scheme) or alpha-addition takes place.


Authors: Wu, B., Szymanski, W., Wybenga, G.G., Heberling, M.M., Bartsch, S., Wildeman, S., Poelarends, G.J., Feringa, B.L., Dijkstra, B.W., Janssen, D.B.
Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates.,Wu B, Szymanski W, Wybenga GG, Heberling MM, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB Angew Chem Int Ed Engl. 2012 Jan 9;51(2):482-6. doi: 10.1002/anie.201106372. Epub, 2011 Nov 23. PMID:22113970<ref>PMID:22113970</ref>


Description: Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yii" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Aminomutase 3D structures|Aminomutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Taxus chinensis]]
[[Category: Bartsch S]]
[[Category: Dijkstra BW]]
[[Category: Feringa BL]]
[[Category: Heberling MM]]
[[Category: Janssen DB]]
[[Category: Poelarends GJ]]
[[Category: Szymanski W]]
[[Category: Wildeman S]]
[[Category: Wu B]]
[[Category: Wybenga GG]]

Latest revision as of 11:14, 23 August 2023

Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolutionManipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution

Structural highlights

2yii is a 4 chain structure with sequence from Taxus chinensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.18Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAM_TAXWC Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first commited step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.[1] [2] [3]

Publication Abstract from PubMed

Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regioselective amination of cinnamate derivatives (see scheme, red) to, for example, beta-amino acids. This regioselectivity, along with the X-ray crystal structures, suggests two distinct carboxylate binding modes differentiated by C(beta)-C(ipso) bond rotation, which determines if beta- (see scheme) or alpha-addition takes place.

Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates.,Wu B, Szymanski W, Wybenga GG, Heberling MM, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB Angew Chem Int Ed Engl. 2012 Jan 9;51(2):482-6. doi: 10.1002/anie.201106372. Epub, 2011 Nov 23. PMID:22113970[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Steele CL, Chen Y, Dougherty BA, Li W, Hofstead S, Lam KS, Xing Z, Chiang SJ. Purification, cloning, and functional expression of phenylalanine aminomutase: the first committed step in Taxol side-chain biosynthesis. Arch Biochem Biophys. 2005 Jun 1;438(1):1-10. PMID:15878763 doi:http://dx.doi.org/10.1016/j.abb.2005.04.012
  2. ↑ Wu B, Szymanski W, Wybenga GG, Heberling MM, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB. Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates. Angew Chem Int Ed Engl. 2012 Jan 9;51(2):482-6. doi: 10.1002/anie.201106372. Epub, 2011 Nov 23. PMID:22113970 doi:http://dx.doi.org/10.1002/anie.201106372
  3. ↑ Wybenga GG, Szymanski W, Wu B, Feringa BL, Janssen DB, Dijkstra BW. Structural Investigations into the Stereochemistry and Activity of a Phenylalanine-2,3-aminomutase from Taxus chinensis. Biochemistry. 2014 May 12. PMID:24786474 doi:http://dx.doi.org/10.1021/bi500187a
  4. ↑ Wu B, Szymanski W, Wybenga GG, Heberling MM, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB. Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates. Angew Chem Int Ed Engl. 2012 Jan 9;51(2):482-6. doi: 10.1002/anie.201106372. Epub, 2011 Nov 23. PMID:22113970 doi:http://dx.doi.org/10.1002/anie.201106372

2yii, resolution 2.18Å

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