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| | <StructureSection load='6tor' size='340' side='right'caption='[[6tor]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='6tor' size='340' side='right'caption='[[6tor]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tor]] is a 2 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=6TOR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TOR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tor]] is a 2 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=6TOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TOR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETNPPL, AGXT2L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ethanolamine-phosphate_phospho-lyase Ethanolamine-phosphate phospho-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.2 4.2.3.2] </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=6tor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tor OCA], [https://pdbe.org/6tor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tor RCSB], [https://www.ebi.ac.uk/pdbsum/6tor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tor 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=6tor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tor OCA], [http://pdbe.org/6tor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tor RCSB], [http://www.ebi.ac.uk/pdbsum/6tor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tor ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AT2L1_HUMAN AT2L1_HUMAN]] Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.<ref>PMID:22241472</ref> | + | [https://www.uniprot.org/uniprot/AT2L1_HUMAN AT2L1_HUMAN] Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.<ref>PMID:22241472</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: Ethanolamine-phosphate phospho-lyase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Donini, S]] | + | [[Category: Donini S]] |
| - | [[Category: Parisini, E]] | + | [[Category: Parisini E]] |
| - | [[Category: Vettraino, C]] | + | [[Category: Vettraino C]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: O-phosphoethanolamine phospho-lyase]]
| + | |
| - | [[Category: Phospholipid metabolism]]
| + | |
| - | [[Category: Pyridoxal 5'-phosphate-dependent enzyme]]
| + | |
| Structural highlights
Function
AT2L1_HUMAN Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde.[1]
Publication Abstract from PubMed
Human O-phosphoethanolamine phospho-lyase (hEtnppl; EC 4.2.3.2) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the degradation of O-phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia. Physiologically, the enzyme is involved in phospholipid metabolism, as PEA is the precursor of phosphatidylethanolamine in the CDP-ethanolamine (Kennedy) pathway. Here, the crystal structure of hEtnppl in complex with pyridoxamine 5'-phosphate was determined at 2.05 A resolution by molecular replacement using the structure of A1RDF1 from Arthrobacter aurescens TC1 (PDB entry 5g4i) as the search model. Structural analysis reveals that the two proteins share the same general fold and a similar arrangement of active-site residues. These results provide novel and useful information for the complete characterization of the human enzyme.
Structural characterization of human O-phosphoethanolamine phospho-lyase.,Vettraino C, Peracchi A, Donini S, Parisini E Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):160-167. doi:, 10.1107/S2053230X20002988. Epub 2020 Apr 1. PMID:32254049[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Veiga-da-Cunha M, Hadi F, Balligand T, Stroobant V, Van Schaftingen E. Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine. J Biol Chem. 2012 Mar 2;287(10):7246-55. doi: 10.1074/jbc.M111.323485. Epub 2012 , Jan 12. PMID:22241472 doi:http://dx.doi.org/10.1074/jbc.M111.323485
- ↑ Vettraino C, Peracchi A, Donini S, Parisini E. Structural characterization of human O-phosphoethanolamine phospho-lyase. Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):160-167. doi:, 10.1107/S2053230X20002988. Epub 2020 Apr 1. PMID:32254049 doi:http://dx.doi.org/10.1107/S2053230X20002988
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