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| | ==Crystal structure of beta-alanine synthase from Saccharomyces kluyveri in complex with a gly-gly peptide== | | ==Crystal structure of beta-alanine synthase from Saccharomyces kluyveri in complex with a gly-gly peptide== |
| - | <StructureSection load='2vl1' size='340' side='right' caption='[[2vl1]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='2vl1' size='340' side='right'caption='[[2vl1]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vl1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_58438 Atcc 58438]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VL1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vl1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachancea_kluyveri Lachancea kluyveri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VL1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v8v|2v8v]], [[2v8d|2v8d]], [[2v8h|2v8h]], [[2v8g|2v8g]], [[1r43|1r43]], [[1r3n|1r3n]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ureidopropionase Beta-ureidopropionase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.6 3.5.1.6] </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=2vl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vl1 OCA], [https://pdbe.org/2vl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vl1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vl1 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=2vl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vl1 OCA], [http://pdbe.org/2vl1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vl1 RCSB], [http://www.ebi.ac.uk/pdbsum/2vl1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vl1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q96W94_LACKL Q96W94_LACKL] |
| | == 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 58438]] | + | [[Category: Lachancea kluyveri]] |
| - | [[Category: Beta-ureidopropionase]] | + | [[Category: Large Structures]] |
| - | [[Category: Andersen, B]] | + | [[Category: Andersen B]] |
| - | [[Category: Dobritzsch, D]] | + | [[Category: Dobritzsch D]] |
| - | [[Category: Lundgren, S]] | + | [[Category: Lundgren S]] |
| - | [[Category: Piskur, J]] | + | [[Category: Piskur J]] |
| - | [[Category: Alpha and beta protein]]
| + | |
| - | [[Category: Amidohydrolase]]
| + | |
| - | [[Category: Complex with glycine-glycine]]
| + | |
| - | [[Category: Di-zinc center]]
| + | |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
Q96W94_LACKL
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In nature, the same biochemical reaction can be catalyzed by enzymes having fundamentally different folds, reaction mechanisms and origins. For example, the third step of the reductive catabolism of pyrimidines, the conversion of N-carbamyl-beta-alanine to beta-alanine, is catalyzed by two beta-alanine synthase (beta ASase, EC 3.5.1.6) subfamilies. We show that the "prototype" eukaryote beta ASases, such as those from Drosophila melanogaster and Arabidopsis thaliana, are relatively efficient in the conversion of N-carbamyl-beta A compared with a representative of fungal beta ASases, the yeast Saccharomyces kluyveri beta ASase, which has a high K(m) value (71 mM). S. kluyveri beta ASase is specifically inhibited by dipeptides and tripeptides, and the apparent K(i) value of glycyl-glycine is in the same range as the substrate K(m). We show that this inhibitor binds to the enzyme active center in a similar way as the substrate. The observed structural similarities and inhibition behavior, as well as the phylogenetic relationship, suggest that the ancestor of the fungal beta ASase was a protease that had modified its profession and become involved in the metabolism of nucleic acid precursors.
A recruited protease is involved in catabolism of pyrimidines.,Andersen B, Lundgren S, Dobritzsch D, Piskur J J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:18448119[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Andersen B, Lundgren S, Dobritzsch D, Piskur J. A recruited protease is involved in catabolism of pyrimidines. J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:18448119 doi:10.1016/j.jmb.2008.03.073
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