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| | ==Structure of wild type A. niger Fdc1 purified in the dark with prFMN in the iminium form== | | ==Structure of wild type A. niger Fdc1 purified in the dark with prFMN in the iminium form== |
| - | <StructureSection load='6ev4' size='340' side='right' caption='[[6ev4]], [[Resolution|resolution]] 1.14Å' scene=''> | + | <StructureSection load='6ev4' size='340' side='right'caption='[[6ev4]], [[Resolution|resolution]] 1.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ev4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspnc Aspnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EV4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ev4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger_CBS_513.88 Aspergillus niger CBS 513.88]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EV4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4LU:1-DEOXY-5-O-PHOSPHONO-1-(3,3,4,5-TETRAMETHYL-9,11-DIOXO-2,3,8,9,10,11-HEXAHYDRO-7H-QUINOLINO[1,8-FG]PTERIDIN-12-IUM-7-YL)-D-RIBITOL'>4LU</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fdc1, An03g06590 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=425011 ASPNC])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4LU:1-DEOXY-5-O-PHOSPHONO-1-(3,3,4,5-TETRAMETHYL-9,11-DIOXO-2,3,8,9,10,11-HEXAHYDRO-7H-QUINOLINO[1,8-FG]PTERIDIN-12-IUM-7-YL)-D-RIBITOL'>4LU</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenacrylate_decarboxylase Phenacrylate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.102 4.1.1.102] </span></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=6ev4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ev4 OCA], [https://pdbe.org/6ev4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ev4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ev4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ev4 ProSAT]</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=6ev4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ev4 OCA], [http://pdbe.org/6ev4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ev4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ev4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ev4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FDC1_ASPNC FDC1_ASPNC]] Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.[HAMAP-Rule:MF_03196]<ref>PMID:26083754</ref> | + | [https://www.uniprot.org/uniprot/FDC1_ASPNC FDC1_ASPNC] Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.[HAMAP-Rule:MF_03196]<ref>PMID:26083754</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspnc]] | + | [[Category: Aspergillus niger CBS 513 88]] |
| - | [[Category: Phenacrylate decarboxylase]] | + | [[Category: Large Structures]] |
| - | [[Category: Bailey, S S]] | + | [[Category: Bailey SS]] |
| - | [[Category: David, L]] | + | [[Category: David L]] |
| - | [[Category: Payne, K A.P]] | + | [[Category: Payne KAP]] |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
FDC1_ASPNC Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.[HAMAP-Rule:MF_03196][1]
Publication Abstract from PubMed
The UbiD family of reversible decarboxylases act on aromatic, heteroaromatic, and unsaturated aliphatic acids and utilize a prenylated flavin mononucleotide (prFMN) as cofactor, bound adjacent to a conserved Glu-ArgGlu/Asp ionic network in the enzyme's active site. It is proposed that UbiD activation requires oxidative maturation of the cofactor, for which two distinct isomers, prFMN(ketimine) and prFMN(iminium) have been observed. It also has been suggested that only the prFMN(iminium) form is relevant to catalysis, which requires transient cycloaddition between substrate and cofactor. Using Aspergillus niger Fdc1 as a model system, we reveal isomerization of prFMN(iminium) to prFMN(ketimine) is a light-dependent process that is largely independent of the Glu277-Arg173-Glu282 network and accompanied by irreversible loss of activity. On the other hand, efficient catalysis was highly dependent on an intact Glu-Ar-Glu network, as only Glu to Asp substitutions retain activity. Surprisingly, oxidative maturation to form the prFMN(iminium) species is severely affected only for the R173A variant. In summary, the unusual irreversible isomerization of prFMN is light dependent and likely proceeds via high-energy intermediates, but is independent of the Glu-Arg-Glu network. Our results from mutagenesis, crystallographic, spectroscopic and kinetic experiments indicate a clear role for the Glu-Arg-Glu network in both catalysis and oxidative maturation.
The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerisation and catalysis.,Bailey SS, Payne KAP, Fisher K, Marshall SA, Cliff MJ, Spiess R, Parker DA, Rigby SE, Leys D J Biol Chem. 2017 Dec 19. pii: RA117.000881. doi: 10.1074/jbc.RA117.000881. PMID:29259125[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Payne KA, White MD, Fisher K, Khara B, Bailey SS, Parker D, Rattray NJ, Trivedi DK, Goodacre R, Beveridge R, Barran P, Rigby SE, Scrutton NS, Hay S, Leys D. New cofactor supports alpha,beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature. 2015 Jun 25;522(7557):497-501. doi: 10.1038/nature14560. Epub 2015 Jun, 17. PMID:26083754 doi:http://dx.doi.org/10.1038/nature14560
- ↑ Bailey SS, Payne KAP, Fisher K, Marshall SA, Cliff MJ, Spiess R, Parker DA, Rigby SE, Leys D. The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerisation and catalysis. J Biol Chem. 2017 Dec 19. pii: RA117.000881. doi: 10.1074/jbc.RA117.000881. PMID:29259125 doi:http://dx.doi.org/10.1074/jbc.RA117.000881
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