6evd - Revision history

OCA at 06:05, 3 January 2018

2018-01-03T06:05:55Z

← Older revision		Revision as of 06:05, 3 January 2018
Line 11:		Line 11:
	== 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>		[[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>
			<div style="background-color:#fffaf0;">
			== 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<ref>PMID:29259125</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 6evd" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:02, 27 December 2017

2017-12-27T09:02:03Z

← Older revision		Revision as of 09:02, 27 December 2017
Line 3:		Line 3:
	<StructureSection load='6evd' size='340' side='right' caption='[[6evd]], [[Resolution\|resolution]] 1.19Å' scene=''>		<StructureSection load='6evd' size='340' side='right' caption='[[6evd]], [[Resolution\|resolution]] 1.19Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6evd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EVD FirstGlance]. <br>		<table><tr><td colspan='2'>[[6evd]] 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=6EVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EVD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BYN:hydroxylated+prenyl-FMN'>BYN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BYN:hydroxylated+prenyl-FMN'>BYN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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='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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6evd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evd OCA], [http://pdbe.org/6evd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6evd RCSB], [http://www.ebi.ac.uk/pdbsum/6evd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6evd 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=6evd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evd OCA], [http://pdbe.org/6evd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6evd RCSB], [http://www.ebi.ac.uk/pdbsum/6evd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6evd ProSAT]</span></td></tr>
Line 14:		Line 15:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Aspnc]]
	[[Category: Phenacrylate decarboxylase]]		[[Category: Phenacrylate decarboxylase]]
	[[Category: Bailey, S S]]		[[Category: Bailey, S S]]

OCA at 06:28, 20 December 2017

2017-12-20T06:28:17Z

← Older revision		Revision as of 06:28, 20 December 2017
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 6evd is ~~ON HOLD~~		==Structure of R173A A. niger Fdc1 with prFMN in the hydroxylated form==
			<StructureSection load='6evd' size='340' side='right' caption='[[6evd]], [[Resolution\|resolution]] 1.19Å' scene=''>
	~~Authors~~: ~~Bailey~~, S.S., ~~David~~, L., ~~Payne~~, K.A.P.		== Structural highlights ==
			<table><tr><td colspan='2'>[[6evd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EVD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EVD FirstGlance]. <br>
	~~Description~~: ~~Structure~~ of ~~R173A A~~. ~~niger Fdc1 with prFMN in the hydroxylated form~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BYN:hydroxylated+prenyl-FMN'>BYN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	[~~[Category~~: ~~Unreleased Structures]~~]		<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>
	[[Category: ~~Payne, K.A.P~~]]		<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=6evd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6evd OCA], [http://pdbe.org/6evd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6evd RCSB], [http://www.ebi.ac.uk/pdbsum/6evd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6evd ProSAT]</span></td></tr>
	[[Category: Bailey, S.S]]		</table>
			== 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>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Phenacrylate decarboxylase]]
			[[Category: Bailey, S S]]
	[[Category: David, L]]		[[Category: David, L]]
			[[Category: Payne, K A.P]]
			[[Category: Lyase]]

OCA: Protected "6evd" [edit=sysop:move=sysop]

2017-11-08T06:44:37Z

Protected "6evd" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:44, 8 November 2017
(No difference)

OCA: New page: '''Unreleased structure''' The entry 6evd is ON HOLD Authors: Bailey, S.S., David, L., Payne, K.A.P. Description: Structure of R173A A. niger Fdc1 with prFMN in the hydroxylated form [...

2017-11-08T06:44:36Z

New page: '''Unreleased structure''' The entry 6evd is ON HOLD Authors: Bailey, S.S., David, L., Payne, K.A.P. Description: Structure of R173A A. niger Fdc1 with prFMN in the hydroxylated form [...

New page

'''Unreleased structure'''

The entry 6evd is ON HOLD

Authors: Bailey, S.S., David, L., Payne, K.A.P.

Description: Structure of R173A A. niger Fdc1 with prFMN in the hydroxylated form
[[Category: Unreleased Structures]]
[[Category: Payne, K.A.P]]
[[Category: Bailey, S.S]]
[[Category: David, L]]