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| | ==Benzophenone synthase from Hypericum androsaemum== | | ==Benzophenone synthase from Hypericum androsaemum== |
| - | <StructureSection load='5uco' size='340' side='right' caption='[[5uco]], [[Resolution|resolution]] 2.85Å' scene=''> | + | <StructureSection load='5uco' size='340' side='right'caption='[[5uco]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uco]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UCO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uco]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UCO FirstGlance]. <br> |
| | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,3',4,6-tetrahydroxybenzophenone_synthase 2,3',4,6-tetrahydroxybenzophenone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.151 2.3.1.151] </span></td></tr> | | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,3',4,6-tetrahydroxybenzophenone_synthase 2,3',4,6-tetrahydroxybenzophenone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.151 2.3.1.151] </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=5uco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uco OCA], [http://pdbe.org/5uco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uco RCSB], [http://www.ebi.ac.uk/pdbsum/5uco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uco ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5uco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uco OCA], [http://pdbe.org/5uco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uco RCSB], [http://www.ebi.ac.uk/pdbsum/5uco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uco ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: 2,3',4,6-tetrahydroxybenzophenone synthase]] | | [[Category: 2,3',4,6-tetrahydroxybenzophenone synthase]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Jr, C E.Stewart]] | | [[Category: Jr, C E.Stewart]] |
| | [[Category: Noel, J P]] | | [[Category: Noel, J P]] |
| Structural highlights
Function
[TBSYN_HYPAN] Type III polyketide synthase involved in the biosynthesis of benzophenones and xanthones. The preferred substrate is benzoyl-CoA, but can also use 3-hydroxybenzoyl-CoA with a lower activity.[1] [2] [3]
Publication Abstract from PubMed
Biphenyl synthase and benzophenone synthase constitute an evolutionarily distinct clade of type III polyketide synthases (PKSs) that use benzoic acid-derived substrates to produce defense metabolites in plants. The use of benzoyl-CoA as an endogenous substrate is unusual for type III PKSs. Moreover, sequence analyses indicate that the residues responsible for the functional diversification of type III PKSs are mutated in benzoic acid-specific type III PKSs. In order to gain a better understanding of structure-function relationships within the type III PKS family, the crystal structures of biphenyl synthase from Malus x domestica and benzophenone synthase from Hypericum androsaemum were compared with the structure of an archetypal type III PKS: chalcone synthase from Malus x domestica. Both biphenyl synthase and benzophenone synthase contain mutations that reshape their active-site cavities to prevent the binding of 4-coumaroyl-CoA and to favor the binding of small hydrophobic substrates. The active-site cavities of biphenyl synthase and benzophenone synthase also contain a novel pocket associated with their chain-elongation and cyclization reactions. Collectively, these results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants.
Molecular architectures of benzoic acid-specific type III polyketide synthases.,Stewart C Jr, Woods K, Macias G, Allan AC, Hellens RP, Noel JP Acta Crystallogr D Struct Biol. 2017 Dec 1;73(Pt 12):1007-1019. doi:, 10.1107/S2059798317016618. Epub 2017 Nov 30. PMID:29199980[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu B, Falkenstein-Paul H, Schmidt W, Beerhues L. Benzophenone synthase and chalcone synthase from Hypericum androsaemum cell cultures: cDNA cloning, functional expression, and site-directed mutagenesis of two polyketide synthases. Plant J. 2003 Jun;34(6):847-55. PMID:12795704
- ↑ Klundt T, Bocola M, Lutge M, Beuerle T, Liu B, Beerhues L. A single amino acid substitution converts benzophenone synthase into phenylpyrone synthase. J Biol Chem. 2009 Nov 6;284(45):30957-64. doi: 10.1074/jbc.M109.038927. Epub 2009, Aug 26. PMID:19710020 doi:http://dx.doi.org/10.1074/jbc.M109.038927
- ↑ Schmidt W, Beerhues L. Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum L. FEBS Lett. 1997 Dec 29;420(2-3):143-6. PMID:9459298
- ↑ Stewart C Jr, Woods K, Macias G, Allan AC, Hellens RP, Noel JP. Molecular architectures of benzoic acid-specific type III polyketide synthases. Acta Crystallogr D Struct Biol. 2017 Dec 1;73(Pt 12):1007-1019. doi:, 10.1107/S2059798317016618. Epub 2017 Nov 30. PMID:29199980 doi:http://dx.doi.org/10.1107/S2059798317016618
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