|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with phenylethylamine.== | | ==Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with phenylethylamine.== |
| - | <StructureSection load='2hkm' size='340' side='right' caption='[[2hkm]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='2hkm' size='340' side='right'caption='[[2hkm]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hkm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HKM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hkm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HKM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</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]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hj4|2hj4]], [[2hj7|2hj7]], [[2hjb|2hjb]], [[2hkr|2hkr]]</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=2hkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkm OCA], [https://pdbe.org/2hkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hkm RCSB], [https://www.ebi.ac.uk/pdbsum/2hkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hkm 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/Aralkylamine_dehydrogenase_(azurin) Aralkylamine dehydrogenase (azurin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.2 1.4.9.2] </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=2hkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkm OCA], [http://pdbe.org/2hkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hkm RCSB], [http://www.ebi.ac.uk/pdbsum/2hkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hkm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AAUA_ALCFA AAUA_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:7876189</ref> <ref>PMID:17087503</ref> <ref>PMID:17005560</ref> <ref>PMID:16614214</ref> [[http://www.uniprot.org/uniprot/AAUB_ALCFA AAUB_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:16614214</ref> | + | [https://www.uniprot.org/uniprot/AAUA_ALCFA AAUA_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:7876189</ref> <ref>PMID:17087503</ref> <ref>PMID:17005560</ref> <ref>PMID:16614214</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 17: |
Line 15: |
| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hk/2hkm_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hk/2hkm_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 24: |
Line 22: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Aromatic amine dehydrogenase|Aromatic amine dehydrogenase]] | + | *[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 30: |
Line 28: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Alcaligenes faecalis]] | | [[Category: Alcaligenes faecalis]] |
| - | [[Category: Leys, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Roujeinikova, A]] | + | [[Category: Leys D]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Roujeinikova A]] |
| Structural highlights
Function
AAUA_ALCFA Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Chistoserdov AY. Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology. 2001 Aug;147(Pt 8):2195-202. PMID:11495996
- ↑ Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. FEBS J. 2005 Nov;272(22):5894-909. PMID:16279953 doi:http://dx.doi.org/EJB4990
- ↑ Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. PMID:8188594
- ↑ Edwards SL, Davidson VL, Hyun YL, Wingfield PT. Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J Biol Chem. 1995 Mar 3;270(9):4293-8. PMID:7876189
- ↑ Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503 doi:http://dx.doi.org/10.1021/bi0612972
- ↑ Roujeinikova A, Scrutton NS, Leys D. Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase. J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. PMID:17005560 doi:http://dx.doi.org/10.1074/jbc.M605559200
- ↑ Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D. Atomic description of an enzyme reaction dominated by proton tunneling. Science. 2006 Apr 14;312(5771):237-41. PMID:16614214 doi:312/5771/237
|
