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| | <StructureSection load='5fjn' size='340' side='right'caption='[[5fjn]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='5fjn' size='340' side='right'caption='[[5fjn]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fjn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19692 Atcc 19692]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fjn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_myxofaciens Proteus myxofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FJN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fjm|5fjm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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=5fjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjn OCA], [http://pdbe.org/5fjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fjn RCSB], [http://www.ebi.ac.uk/pdbsum/5fjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjn ProSAT]</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=5fjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjn OCA], [https://pdbe.org/5fjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fjn RCSB], [https://www.ebi.ac.uk/pdbsum/5fjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A158RFS7_9GAMM A0A158RFS7_9GAMM] |
| | <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: Atcc 19692]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Molla, G]] | + | [[Category: Proteus myxofaciens]] |
| - | [[Category: Motta, P]] | + | [[Category: Molla G]] |
| - | [[Category: Nardini, M]] | + | [[Category: Motta P]] |
| - | [[Category: Pollegioni, L]] | + | [[Category: Nardini M]] |
| - | [[Category: Flavoenzyme]]
| + | [[Category: Pollegioni L]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: L-amino acid deaminase]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
A0A158RFS7_9GAMM
Publication Abstract from PubMed
l-Amino acid deaminase from Proteus myxofaciens (PmaLAAD) is a membrane flavoenzyme that catalyzes the deamination of neutral and aromatic l-amino acids into alpha-keto acids and ammonia. PmaLAAD does not use dioxygen to re-oxidize reduced FADH2 and thus does not produce hydrogen peroxide; instead, it uses a cytochrome b-like protein as an electron acceptor. Although the overall fold of this enzyme resembles that of known amine or amino acid oxidases, it shows the following specific structural features: an additional novel alpha+beta subdomain placed close to the putative transmembrane alpha-helix and to the active-site entrance; an FAD isoalloxazine ring exposed to solvent; and a large and accessible active site suitable to bind large hydrophobic substrates. In addition, PmaLAAD requires substrate-induced conformational changes of part of the active site, particularly in Arg-316 and Phe-318, to achieve the correct geometry for catalysis. These studies are expected to pave the way for rationally improving the versatility of this flavoenzyme, which is critical for biocatalysis of enantiomerically pure amino acids.
Structure-Function Relationships in l-Amino Acid Deaminase, a Flavoprotein Belonging to a Novel Class of Biotechnologically Relevant Enzymes.,Motta P, Molla G, Pollegioni L, Nardini M J Biol Chem. 2016 May 13;291(20):10457-75. doi: 10.1074/jbc.M115.703819. Epub, 2016 Mar 28. PMID:27022028[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Motta P, Molla G, Pollegioni L, Nardini M. Structure-Function Relationships in l-Amino Acid Deaminase, a Flavoprotein Belonging to a Novel Class of Biotechnologically Relevant Enzymes. J Biol Chem. 2016 May 13;291(20):10457-75. doi: 10.1074/jbc.M115.703819. Epub, 2016 Mar 28. PMID:27022028 doi:http://dx.doi.org/10.1074/jbc.M115.703819
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