2vk8 - Revision history

OCA at 15:22, 13 December 2023

OCA — Wed, 13 Dec 2023 15:22:42 GMT

←Older revision		Revision as of 15:22, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2vk8' size='340' side='right'caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>		<StructureSection load='2vk8' size='340' side='right'caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=2OP:(2S)~~-~~2-HYDROXYPROPANOIC+ACID'>2OP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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]] 1.42Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class="sblockDat"><span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1]~~ </~~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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [https://pdbe.org/2vk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [https://www.ebi.ac.uk/pdbsum/2vk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vk8 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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [~~http~~://pdbe.org/2vk8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vk8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vk8 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PDC1_YEAST PDC1_YEAST]] Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.<ref>PMID:4687392</ref> <ref>PMID:8866484</ref> <ref>PMID:9341119</ref> <ref>PMID:9748245</ref> <ref>PMID:10234824</ref> <ref>PMID:10231381</ref> <ref>PMID:10753893</ref> <ref>PMID:11141278</ref> <ref>PMID:12499363</ref> <ref>PMID:12902239</ref>	+	[https://www.uniprot.org/uniprot/PDC1_YEAST PDC1_YEAST] Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.<ref>PMID:4687392</ref> <ref>PMID:8866484</ref> <ref>PMID:9341119</ref> <ref>PMID:9748245</ref> <ref>PMID:10234824</ref> <ref>PMID:10231381</ref> <ref>PMID:10753893</ref> <ref>PMID:11141278</ref> <ref>PMID:12499363</ref> <ref>PMID:12902239</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 18824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pyruvate decarboxylase~~]]	+	[[Category: Saccharomyces cerevisiae]]
-	[[Category: Konig, S]]	+	[[Category: Konig S]]
-	[[Category: Kutter, S]]	+	[[Category: Kutter S]]
-	[[Category: Weik, M]]	+	[[Category: Weik M]]
-	[[Category: Weiss~~, M S]]~~	+	[[Category: Weiss MS]]
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Allosteric enzyme]]~~	+
-	~~[[Category: Asymmetric active site]]~~	+
-	~~[[Category: Branched-chain amino acid catabolism]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Decarboxylase]]~~	+
-	~~[[Category: Dimer of dimer]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Magnesium]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Phenylalanine catabolism]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Pyruvate]]~~	+
-	~~[[Category: Substrate activation]]~~	+
-	~~[[Category: Tdp]]~~	+
-	~~[[Category: Thiamine diphosphate]]~~	+
-	~~[[Category: Thiamine pyrophosphate]]~~	+
-	~~[[Category: Tpp]]~~	+
-	~~[[Category: Tryptophan catabolism~~]]	+

OCA at 07:58, 4 November 2020

OCA — Wed, 04 Nov 2020 07:58:38 GMT

←Older revision		Revision as of 07:58, 4 November 2020
Line 1:		Line 1:

	==Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate==		==Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate==
-	<StructureSection load='2vk8' size='340' side='right' caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>	+	<StructureSection load='2vk8' size='340' side='right'caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://pdbe.org/2vk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vk8 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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://pdbe.org/2vk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vk8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</StructureSection>		</StructureSection>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
		+	[[Category: Large Structures]]
	[[Category: Pyruvate decarboxylase]]		[[Category: Pyruvate decarboxylase]]
	[[Category: Konig, S]]		[[Category: Konig, S]]

OCA at 21:13, 19 September 2018

OCA — Wed, 19 Sep 2018 21:13:14 GMT

←Older revision		Revision as of 21:13, 19 September 2018
Line 1:		Line 1:
		+
	==Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate==		==Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate==
	<StructureSection load='2vk8' size='340' side='right' caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>		<StructureSection load='2vk8' size='340' side='right' caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://pdbe.org/2vk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum]</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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://pdbe.org/2vk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vk8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/2vk8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/2vk8_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 42:		Line 43:
	[[Category: Weik, M]]		[[Category: Weik, M]]
	[[Category: Weiss, M S]]		[[Category: Weiss, M S]]
		+	[[Category: Acetylation]]
	[[Category: Allosteric enzyme]]		[[Category: Allosteric enzyme]]
	[[Category: Asymmetric active site]]		[[Category: Asymmetric active site]]
	[[Category: Branched-chain amino acid catabolism]]		[[Category: Branched-chain amino acid catabolism]]
		+	[[Category: Cytoplasm]]
	[[Category: Decarboxylase]]		[[Category: Decarboxylase]]
	[[Category: Dimer of dimer]]		[[Category: Dimer of dimer]]

OCA at 03:15, 7 February 2016

OCA — Sun, 07 Feb 2016 03:15:15 GMT

←Older revision		Revision as of 03:15, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='2vk8' size='340' side='right' caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>		<StructureSection load='2vk8' size='340' side='right' caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae Saccharomyces cerevisiae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum]</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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://pdbe.org/2vk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vk8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2vk8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 18824]]
	[[Category: Pyruvate decarboxylase]]		[[Category: Pyruvate decarboxylase]]
-	[[Category: Saccharomyces cerevisiae]]
	[[Category: Konig, S]]		[[Category: Konig, S]]
	[[Category: Kutter, S]]		[[Category: Kutter, S]]

OCA at 07:24, 24 December 2014

OCA — Wed, 24 Dec 2014 07:24:47 GMT

←Older revision		Revision as of 07:24, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum]</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=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PDC1_YEAST PDC1_YEAST]] Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.<ref>PMID:4687392</ref> <ref>PMID:8866484</ref> <ref>PMID:9341119</ref> <ref>PMID:9748245</ref> <ref>PMID:10234824</ref> <ref>PMID:10231381</ref> <ref>PMID:10753893</ref> <ref>PMID:11141278</ref> <ref>PMID:12499363</ref> <ref>PMID:12902239</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Pyruvate decarboxylase]]		[[Category: Pyruvate decarboxylase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	[[Category: Konig, S.]]	+	[[Category: Konig, S]]
-	[[Category: Kutter, S.]]	+	[[Category: Kutter, S]]
-	[[Category: Weik, M.]]	+	[[Category: Weik, M]]
-	[[Category: Weiss, M S.]]	+	[[Category: Weiss, M S]]
	[[Category: Allosteric enzyme]]		[[Category: Allosteric enzyme]]
	[[Category: Asymmetric active site]]		[[Category: Asymmetric active site]]

OCA at 04:22, 3 October 2014

OCA — Fri, 03 Oct 2014 04:22:21 GMT

←Older revision		Revision as of 04:22, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2vk8\| PDB=2vk8 \| SCENE= }}~~	+	==Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate==
-	===Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate===	+	<StructureSection load='2vk8' size='340' side='right' caption='[[2vk8]], [[Resolution\|resolution]] 1.42Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19246454}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VK8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pyd\|1pyd]], [[2vk1\|2vk1]], [[1pvd\|1pvd]], [[1qpb\|1qpb]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vk8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vk8 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/2vk8_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast species, three of them reported here for the first time, provide detailed atomic resolution snapshots along the activation coordinate. The prime event is the covalent binding of the substrate pyruvate to the side chain of cysteine 221, thus forming a thiohemiketal. This reaction causes the shift of a neighboring amino acid, which eventually leads to the rigidification of two otherwise flexible loops, one of which provides two histidine residues necessary to complete the enzymatically competent active site architecture. The structural data are complemented and supported by kinetic investigations and binding studies, providing a consistent picture of the structural changes occurring upon enzyme activation.

-	~~==Function==~~	+	Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation.,Kutter S, Weiss MS, Wille G, Golbik R, Spinka M, Konig S J Biol Chem. 2009 May 1;284(18):12136-44. Epub 2009 Feb 26. PMID:19246454<ref>PMID:19246454</ref>
-	~~[[http://www.uniprot.org/uniprot/PDC1_YEAST PDC1_YEAST]] Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in~~ the ~~nonoxidative conversion~~ of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases ~~(PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the~~ enzyme ~~catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids~~. ~~In a third step~~, ~~the resulting aldehydes are reduced to alcohols~~, ~~collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine~~, ~~isoleucine~~, ~~phenylalanine~~, ~~and tryptophan~~, ~~whereas leucine is no substrate~~. ~~In a side-reaction the carbanionic intermediate~~ (~~or active aldehyde~~) ~~generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2~~-~~hydroxy ketone, collectively called acyloins~~.~~<ref>~~PMID:4687392</ref> <ref>PMID:8866484</ref> <ref>PMID:9341119</ref> <ref>PMID:9748245</ref> <ref>PMID:10234824</ref> <ref>PMID:10231381</ref> <ref>PMID:10753893</ref> <ref>PMID:11141278</ref> <ref>PMID:12499363</ref> <ref>PMID:~~12902239~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[2vk8]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Pyruvate decarboxylase\|Pyruvate decarboxylase]]		*[[Pyruvate decarboxylase\|Pyruvate decarboxylase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019246454</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Pyruvate decarboxylase]]		[[Category: Pyruvate decarboxylase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]

OCA at 04:20, 12 September 2013

OCA — Thu, 12 Sep 2013 04:20:57 GMT

←Older revision		Revision as of 04:20, 12 September 2013
Line 1:		Line 1:
-	[[Image:2vk8.png\|left\|200px]]
-
	{{STRUCTURE_2vk8\| PDB=2vk8 \| SCENE= }}		{{STRUCTURE_2vk8\| PDB=2vk8 \| SCENE= }}
		+	===Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate===
		+	{{ABSTRACT_PUBMED_19246454}}

-	===~~CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT E477Q IN COMPLEX WITH ITS SUBSTRATE~~===	+	==Function==
-		+	[[http://www.uniprot.org/uniprot/PDC1_YEAST PDC1_YEAST]] Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.<ref>PMID:4687392</ref> <ref>PMID:8866484</ref> <ref>PMID:9341119</ref> <ref>PMID:9748245</ref> <ref>PMID:10234824</ref> <ref>PMID:10231381</ref> <ref>PMID:10753893</ref> <ref>PMID:11141278</ref> <ref>PMID:12499363</ref> <ref>PMID:12902239</ref>
-	~~{{ABSTRACT_PUBMED_19246454}}~~	+

	==About this Structure==		==About this Structure==
Line 14:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019246454</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019246454</ref><references group="xtra"/><references/>
	[[Category: Pyruvate decarboxylase]]		[[Category: Pyruvate decarboxylase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]

OCA at 05:26, 20 October 2012

OCA — Sat, 20 Oct 2012 05:26:24 GMT

←Older revision		Revision as of 05:26, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2vk8]] is a 4 chain structure ~~of [[Pyruvate decarboxylase]]~~ with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA].	+	[[2vk8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA].

	==See Also==		==See Also==

OCA: Protected "2vk8" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 10:01:48 GMT

Protected "2vk8" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:01, 25 July 2012

OCA at 10:01, 25 July 2012

OCA — Wed, 25 Jul 2012 10:01:46 GMT

←Older revision		Revision as of 10:01, 25 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2vk8.png\|left\|200px]]		[[Image:2vk8.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2vk8", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2vk8\| PDB=2vk8 \| SCENE= }}		{{STRUCTURE_2vk8\| PDB=2vk8 \| SCENE= }}

	===CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT E477Q IN COMPLEX WITH ITS SUBSTRATE===		===CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT E477Q IN COMPLEX WITH ITS SUBSTRATE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19246454}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19246454 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19246454}}		{{ABSTRACT_PUBMED_19246454}}

	==About this Structure==		==About this Structure==
-	~~2VK8~~ is a 4 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA].	+	[[2vk8]] is a 4 chain structure of [[Pyruvate decarboxylase]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VK8 OCA].
		+
		+	==See Also==
		+	*[[Pyruvate decarboxylase\|Pyruvate decarboxylase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19246454~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019246454</ref><references group="xtra"/>
	[[Category: Pyruvate decarboxylase]]		[[Category: Pyruvate decarboxylase]]
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
Line 30:		Line 21:
	[[Category: Weik, M.]]		[[Category: Weik, M.]]
	[[Category: Weiss, M S.]]		[[Category: Weiss, M S.]]
-	[[Category: Acetylation]]
	[[Category: Allosteric enzyme]]		[[Category: Allosteric enzyme]]
	[[Category: Asymmetric active site]]		[[Category: Asymmetric active site]]
	[[Category: Branched-chain amino acid catabolism]]		[[Category: Branched-chain amino acid catabolism]]
-	[[Category: Cytoplasm]]
	[[Category: Decarboxylase]]		[[Category: Decarboxylase]]
	[[Category: Dimer of dimer]]		[[Category: Dimer of dimer]]
Line 50:		Line 39:
	[[Category: Tpp]]		[[Category: Tpp]]
	[[Category: Tryptophan catabolism]]		[[Category: Tryptophan catabolism]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 6 09:26:13 2009''