<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>283(30)</volume><submitter>Emter R</submitter><pubmed_abstract>Human axillary odor is formed by the action of Corynebacteria on odorless axilla secretions. Sulfanylalkanols, 3-methyl-3-sulfanylhexan-1-ol in particular, form one key class of the odoriferous compounds. A conjugate with the dipeptide Cys-Gly has been reported as the secreted precursor for 3-methyl-3-sulfanylhexan-1-ol. Here, we confirm the Cys-Gly-(S) conjugate as the major precursor of this odorant, with lower levels of the Cys-(S) conjugate being present in axilla secretions. The enzymatic release of 3-methyl-3-sulfanylhexan-1-ol from the Cys-Gly-(S) conjugate by the axilla isolate Corynebacterium Ax20 was thus investigated. Cellular extracts of Ax20 released 3-methyl-3-sulfanylhexan-1-ol from the Cys-Gly-(S) conjugate and from the Cys-(S) conjugate, whereas the previously isolated C-S</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>20645-52</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3258934</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The sequential action of a dipeptidase and a beta-lyase is required for the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a secreted Cys-Gly-(S) conjugate by Corynebacteria.</pubmed_title><pmcid>PMC3258934</pmcid><pubmed_authors>Natsch A</pubmed_authors><pubmed_authors>Emter R</pubmed_authors></additional><is_claimable>false</is_claimable><name>The sequential action of a dipeptidase and a beta-lyase is required for the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a secreted Cys-Gly-(S) conjugate by Corynebacteria.</name><description>Human axillary odor is formed by the action of Corynebacteria on odorless axilla secretions. Sulfanylalkanols, 3-methyl-3-sulfanylhexan-1-ol in particular, form one key class of the odoriferous compounds. A conjugate with the dipeptide Cys-Gly has been reported as the secreted precursor for 3-methyl-3-sulfanylhexan-1-ol. Here, we confirm the Cys-Gly-(S) conjugate as the major precursor of this odorant, with lower levels of the Cys-(S) conjugate being present in axilla secretions. The enzymatic release of 3-methyl-3-sulfanylhexan-1-ol from the Cys-Gly-(S) conjugate by the axilla isolate Corynebacterium Ax20 was thus investigated. Cellular extracts of Ax20 released 3-methyl-3-sulfanylhexan-1-ol from the Cys-Gly-(S) conjugate and from the Cys-(S) conjugate, whereas the previously isolated C-S</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Jul</publication><modification>2026-05-04T08:16:59.528Z</modification><creation>2019-03-27T00:48:00Z</creation></dates><accession>S-EPMC3258934</accession><cross_references><pubmed>18515361</pubmed><doi>10.1074/jbc.m800730200</doi><doi>10.1074/jbc.M800730200</doi></cross_references></HashMap>