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| | <StructureSection load='5hsj' size='340' side='right'caption='[[5hsj]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5hsj' size='340' side='right'caption='[[5hsj]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hsj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_casei_g"_von_freudenreich_and_thoni_1904 "bacillus casei g" von freudenreich and thoni 1904]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HSJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HSJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis Levilactobacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HSJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hsi|5hsi]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tdc, N624_0219 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1580 "Bacillus casei g" von Freudenreich and Thoni 1904])</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=5hsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hsj OCA], [https://pdbe.org/5hsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hsj RCSB], [https://www.ebi.ac.uk/pdbsum/5hsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hsj 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/Tyrosine_decarboxylase Tyrosine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.25 4.1.1.25] </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=5hsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hsj OCA], [http://pdbe.org/5hsj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hsj RCSB], [http://www.ebi.ac.uk/pdbsum/5hsj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hsj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TYRDC_LEVBR TYRDC_LEVBR] Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate (PubMed:24211777).<ref>PMID:24211777</ref> <ref>PMID:27292129</ref> Is also able to decarboxylate the Parkinson's disease medication levodopa (L-dopa) to dopamine in vitro.<ref>PMID:24211777</ref> <ref>PMID:27292129</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: Bacillus casei g von freudenreich and thoni 1904]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tyrosine decarboxylase]] | + | [[Category: Levilactobacillus brevis]] |
| - | [[Category: Ni, Y]] | + | [[Category: Ni Y]] |
| - | [[Category: Zhang, K]] | + | [[Category: Zhang K]] |
| - | [[Category: Zhou, J]] | + | [[Category: Zhou J]] |
| - | [[Category: Zhu, H]] | + | [[Category: Zhu H]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Plp]]
| + | |
| Structural highlights
Function
TYRDC_LEVBR Catalyzes the decarboxylation of L-tyrosine to produce tyramine (PubMed:24211777, PubMed:27292129). Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate (PubMed:24211777).[1] [2] Is also able to decarboxylate the Parkinson's disease medication levodopa (L-dopa) to dopamine in vitro.[3] [4]
Publication Abstract from PubMed
Tyrosine decarboxylase (TDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme and is mainly responsible for the synthesis of tyramine, an important biogenic amine. In this study, the crystal structures of the apo and holo forms of Lactobacillus brevis TDC (LbTDC) were determined. The LbTDC displays only 25% sequence identity with the only reported TDC structure. Site-directed mutagenesis of the conformationally flexible sites and catalytic center was performed to investigate the potential catalytic mechanism. It was found that H241 in the active site plays an important role in PLP binding because it has different conformations in the apo and holo structures of LbTDC. After binding to PLP, H241 rotated to the position adjacent to the PLP pyridine ring. Alanine scanning mutagenesis revealed several crucial regions that determine the substrate specificity and catalytic activity. Among the mutants, the S586A variant displayed increased catalytic efficiency and substrate affinity, which is attributed to decreased steric hindrance and increased hydrophobicity, as verified by the saturation mutagenesis at S586. Our results provide structural information about the residues important for the protein engineering of TDC to improve catalytic efficiency in the green manufacturing of tyramine.
Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding.,Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang K, Ni Y. Tyrosine decarboxylase from Lactobacillus brevis: soluble expression and characterization. Protein Expr Purif. 2014 Feb;94:33-9. PMID:24211777 doi:10.1016/j.pep.2013.10.018
- ↑ Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding. Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129 doi:http://dx.doi.org/10.1038/srep27779
- ↑ Zhang K, Ni Y. Tyrosine decarboxylase from Lactobacillus brevis: soluble expression and characterization. Protein Expr Purif. 2014 Feb;94:33-9. PMID:24211777 doi:10.1016/j.pep.2013.10.018
- ↑ Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding. Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129 doi:http://dx.doi.org/10.1038/srep27779
- ↑ Zhu H, Xu G, Zhang K, Kong X, Han R, Zhou J, Ni Y. Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding. Sci Rep. 2016 Jun 13;6:27779. doi: 10.1038/srep27779. PMID:27292129 doi:http://dx.doi.org/10.1038/srep27779
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