<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ze X</submitter><funding>Wellcome Trust</funding><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>e01058-15</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4611034</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>6(5)</volume><pubmed_abstract>&lt;h4>Unlabelled&lt;/h4>Ruminococcus bromii is a dominant member of the human gut microbiota that plays a key role in releasing energy from dietary starches that escape digestion by host enzymes via its exceptional activity against particulate "resistant" starches. Genomic analysis of R. bromii shows that it is highly specialized, with 15 of its 21 glycoside hydrolases belonging to one family (GH13). We found that amylase activity in R. bromii is expressed constitutively, with the activity seen during growth with fructose as an energy source being similar to that seen with starch as an energy source. Six GH13 amylases that carry signal peptides were detected by proteomic analysis in R. bromii cultures. Four of these enzymes are among 26 R. bromii proteins predicted to carry dockerin modules, wi</pubmed_abstract><journal>mBio</journal><pubmed_title>Unique Organization of Extracellular Amylases into Amylosomes in the Resistant Starch-Utilizing Human Colonic Firmicutes Bacterium Ruminococcus bromii.</pubmed_title><pmcid>PMC4611034</pmcid><funding_grant_id>BB/L009951/1</funding_grant_id><funding_grant_id>BB/L008602/1</funding_grant_id><pubmed_authors>Juge N</pubmed_authors><pubmed_authors>Ben David Y</pubmed_authors><pubmed_authors>Laverde-Gomez JA</pubmed_authors><pubmed_authors>Ze X</pubmed_authors><pubmed_authors>Louis P</pubmed_authors><pubmed_authors>Henrissat B</pubmed_authors><pubmed_authors>Flint HJ</pubmed_authors><pubmed_authors>Sheridan PO</pubmed_authors><pubmed_authors>Bayer EA</pubmed_authors><pubmed_authors>Dassa B</pubmed_authors><pubmed_authors>Koropatkin NM</pubmed_authors><pubmed_authors>Duncan SH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Unique Organization of Extracellular Amylases into Amylosomes in the Resistant Starch-Utilizing Human Colonic Firmicutes Bacterium Ruminococcus bromii.</name><description>&lt;h4>Unlabelled&lt;/h4>Ruminococcus bromii is a dominant member of the human gut microbiota that plays a key role in releasing energy from dietary starches that escape digestion by host enzymes via its exceptional activity against particulate "resistant" starches. Genomic analysis of R. bromii shows that it is highly specialized, with 15 of its 21 glycoside hydrolases belonging to one family (GH13). We found that amylase activity in R. bromii is expressed constitutively, with the activity seen during growth with fructose as an energy source being similar to that seen with starch as an energy source. Six GH13 amylases that carry signal peptides were detected by proteomic analysis in R. bromii cultures. Four of these enzymes are among 26 R. bromii proteins predicted to carry dockerin modules, wi</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Sep</publication><modification>2026-05-09T16:24:47.723Z</modification><creation>2019-03-27T02:00:18Z</creation></dates><accession>S-EPMC4611034</accession><cross_references><pubmed>26419877</pubmed><doi>10.1128/mBio.01058-15</doi></cross_references></HashMap>