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| | <StructureSection load='6slf' size='340' side='right'caption='[[6slf]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6slf' size='340' side='right'caption='[[6slf]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6slf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_striatum"_chester_1901 "bacterium striatum" chester 1901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SLF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6slf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_striatum Corynebacterium striatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LJ8:(2~{S})-5-azanyl-2-[[[(3~{S})-3-methyl-5-phenyl-pentyl]-oxidanyl-phosphoryl]methyl]-5-oxidanylidene-pentanoic+acid'>LJ8</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]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">agaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43770 "Bacterium striatum" Chester 1901])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LJ8:(2~{S})-5-azanyl-2-[[[(3~{S})-3-methyl-5-phenyl-pentyl]-oxidanyl-phosphoryl]methyl]-5-oxidanylidene-pentanoic+acid'>LJ8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6slf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6slf OCA], [http://pdbe.org/6slf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6slf RCSB], [http://www.ebi.ac.uk/pdbsum/6slf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6slf 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=6slf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6slf OCA], [https://pdbe.org/6slf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6slf RCSB], [https://www.ebi.ac.uk/pdbsum/6slf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6slf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AGAA_CORST AGAA_CORST] Hydrolyzes odorless N-alpha-acyl-L-glutamine conjugates of short- and medium-chain fatty acids, releasing human axillary malodor compounds (PubMed:12468539, PubMed:18492161, PubMed:17193210). The enzyme is highly specific for the glutamine residue but has a low specificity for the acyl part of the substrate (PubMed:12468539, PubMed:18492161, PubMed:17193210). The two most common products are 3-methyl-2-hexenoic acid (3M2H) and 3-hydroxy-3-methyl-hexanoic acid (HMHA), which are produced from the odorless precursors N-alpha-3-methyl-2-hexenoyl-L-glutamine (3M2H-Gln) and N-alpha-3-hydroxy-3-methylhexanoyl-L-glutamine (HMHA-Gln) (PubMed:12468539, PubMed:18492161, PubMed:17193210). In addition, over 28 different carboxylic acids contributing to human body odor are released by this enzyme from odorless axilla secretions, including several aliphatic 3-hydroxy acids with 4-Me branches, 3,4-unsaturated, 4-Et-branched aliphatic acids, and a variety of degradation products of amino acids (PubMed:17193210).<ref>PMID:12468539</ref> <ref>PMID:17193210</ref> <ref>PMID:18492161</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium striatum chester 1901]] | + | [[Category: Corynebacterium striatum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Emter, R]] | + | [[Category: Emter R]] |
| - | [[Category: Natsch, A]] | + | [[Category: Natsch A]] |
| - | [[Category: Aminoacylase]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Tetramer]]
| + | |
| Structural highlights
6slf is a 4 chain structure with sequence from Corynebacterium striatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.75Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AGAA_CORST Hydrolyzes odorless N-alpha-acyl-L-glutamine conjugates of short- and medium-chain fatty acids, releasing human axillary malodor compounds (PubMed:12468539, PubMed:18492161, PubMed:17193210). The enzyme is highly specific for the glutamine residue but has a low specificity for the acyl part of the substrate (PubMed:12468539, PubMed:18492161, PubMed:17193210). The two most common products are 3-methyl-2-hexenoic acid (3M2H) and 3-hydroxy-3-methyl-hexanoic acid (HMHA), which are produced from the odorless precursors N-alpha-3-methyl-2-hexenoyl-L-glutamine (3M2H-Gln) and N-alpha-3-hydroxy-3-methylhexanoyl-L-glutamine (HMHA-Gln) (PubMed:12468539, PubMed:18492161, PubMed:17193210). In addition, over 28 different carboxylic acids contributing to human body odor are released by this enzyme from odorless axilla secretions, including several aliphatic 3-hydroxy acids with 4-Me branches, 3,4-unsaturated, 4-Et-branched aliphatic acids, and a variety of degradation products of amino acids (PubMed:17193210).[1] [2] [3]
Publication Abstract from PubMed
Human body odour is dominated by the scent of specific odourants emanating from specialized glands in the axillary region. These specific odourants are produced by an intricate interplay between biochemical pathways in the host and odour-releasing enzymes present in commensal microorganisms of the axillary microbiome. Key biochemical steps for the release of highly odouriferous carboxylic acids and sulfur compounds have been elucidated over the past 15 years. Based on the profound molecular understanding and specific analytical methods developed, evolutionary questions could be asked for the first time with small population studies: (i) a genetic basis for body odour could be shown with a twin study, (ii) no effect of genes in the human leukocyte antigen complex on the pattern of odourant carboxylic acid was found, and (iii) loss of odour precursor secretion by a mutation in the ABCC11 gene could explain why a large fraction of the population in the Far East lack body odour formation. This review summarizes what is currently known at the molecular level on the biochemistry of the formation of key odourants in the human axilla. At the same time, we present for the first time the crystal structure of the Nalpha-acyl-aminoacylase, a key human odour-releasing enzyme, thus describing at the molecular level how bacteria on the skin surface have adapted their enzyme to the specific substrates secreted by the human host. This article is part of the Theo Murphy meeting issue 'Olfactory communication in humans'.
The specific biochemistry of human axilla odour formation viewed in an evolutionary context.,Natsch A, Emter R Philos Trans R Soc Lond B Biol Sci. 2020 Jun 8;375(1800):20190269. doi:, 10.1098/rstb.2019.0269. Epub 2020 Apr 20. PMID:32306870[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Natsch A, Gfeller H, Gygax P, Schmid J, Acuna G. A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla. J Biol Chem. 2003 Feb 21;278(8):5718-27. doi: 10.1074/jbc.M210142200. Epub 2002, Dec 4. PMID:12468539 doi:http://dx.doi.org/10.1074/jbc.M210142200
- ↑ Natsch A, Derrer S, Flachsmann F, Schmid J. A broad diversity of volatile carboxylic acids, released by a bacterial aminoacylase from axilla secretions, as candidate molecules for the determination of human-body odor type. Chem Biodivers. 2006 Jan;3(1):1-20. PMID:17193210 doi:10.1002/cbdv.200690015
- ↑ Natsch A, Gfeller H, Gygax P, Schmid J. Isolation of a bacterial enzyme releasing axillary malodor and its use as a screening target for novel deodorant formulations. Int J Cosmet Sci. 2005 Apr;27(2):115-22. PMID:18492161 doi:10.1111/j.1467-2494.2004.00255.x
- ↑ Natsch A, Emter R. The specific biochemistry of human axilla odour formation viewed in an evolutionary context. Philos Trans R Soc Lond B Biol Sci. 2020 Jun 8;375(1800):20190269. doi:, 10.1098/rstb.2019.0269. Epub 2020 Apr 20. PMID:32306870 doi:http://dx.doi.org/10.1098/rstb.2019.0269
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