|
|
| Line 1: |
Line 1: |
| | | | |
| | ==2.39 Angstrom X-ray Crystal structure of human ACMSD== | | ==2.39 Angstrom X-ray Crystal structure of human ACMSD== |
| - | <StructureSection load='4igm' size='340' side='right' caption='[[4igm]], [[Resolution|resolution]] 2.39Å' scene=''> | + | <StructureSection load='4igm' size='340' side='right'caption='[[4igm]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4igm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IGM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4igm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IGM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACMSD, human ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4igm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igm OCA], [https://pdbe.org/4igm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4igm RCSB], [https://www.ebi.ac.uk/pdbsum/4igm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4igm ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminocarboxymuconate-semialdehyde_decarboxylase Aminocarboxymuconate-semialdehyde decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.45 4.1.1.45] </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=4igm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igm OCA], [http://pdbe.org/4igm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4igm RCSB], [http://www.ebi.ac.uk/pdbsum/4igm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4igm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACMSD_HUMAN ACMSD_HUMAN]] Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.<ref>PMID:19843166</ref> <ref>PMID:12140278</ref> | + | [https://www.uniprot.org/uniprot/ACMSD_HUMAN ACMSD_HUMAN] Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.<ref>PMID:19843166</ref> <ref>PMID:12140278</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aminocarboxymuconate-semialdehyde decarboxylase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Liu, A]] | + | [[Category: Liu A]] |
| - | [[Category: Liu, F]] | + | [[Category: Liu F]] |
| - | [[Category: Kynurenine pathway]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Neurological disorder]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| - | [[Category: Zinc-dependent decarboxylase]]
| + | |
| Structural highlights
Function
ACMSD_HUMAN Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.[1] [2]
References
- ↑ Garavaglia S, Perozzi S, Galeazzi L, Raffaelli N, Rizzi M. The crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with 1,3-dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis. FEBS J. 2009 Nov;276(22):6615-23. Epub 2009 Oct 16. PMID:19843166 doi:10.1111/j.1742-4658.2009.07372.x
- ↑ Fukuoka S, Ishiguro K, Yanagihara K, Tanabe A, Egashira Y, Sanada H, Shibata K. Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis". J Biol Chem. 2002 Sep 20;277(38):35162-7. Epub 2002 Jul 24. PMID:12140278 doi:http://dx.doi.org/10.1074/jbc.M200819200
|
