<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Huang X</submitter><funding>NCRR NIH HHS</funding><pagination>10424-10434</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3323023</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>287(13)</volume><pubmed_abstract>Actinomycetes are a group of gram-positive bacteria that includes pathogenic mycobacterial species, such as Mycobacterium tuberculosis. These organisms do not have glutathione and instead utilize the small molecule mycothiol (MSH) as their primary reducing agent and for the detoxification of xenobiotics. Due to these important functions, enzymes involved in MSH biosynthesis and MSH-dependent detoxification are targets for drug development. The metal-dependent deacetylase N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) catalyzes the hydrolysis of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside to form 1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside and acetate in MSH biosynthesis. Herein we examine the chemical mechanism of MshB. We demons</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosine.</pubmed_title><pmcid>PMC3323023</pmcid><funding_grant_id>P41 RR001081</funding_grant_id><pubmed_authors>Hernick M</pubmed_authors><pubmed_authors>Huang X</pubmed_authors></additional><is_claimable>false</is_claimable><name>Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosine.</name><description>Actinomycetes are a group of gram-positive bacteria that includes pathogenic mycobacterial species, such as Mycobacterium tuberculosis. These organisms do not have glutathione and instead utilize the small molecule mycothiol (MSH) as their primary reducing agent and for the detoxification of xenobiotics. Due to these important functions, enzymes involved in MSH biosynthesis and MSH-dependent detoxification are targets for drug development. The metal-dependent deacetylase N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) catalyzes the hydrolysis of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside to form 1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside and acetate in MSH biosynthesis. Herein we examine the chemical mechanism of MshB. We demons</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Mar</publication><modification>2026-05-04T17:53:45.01Z</modification><creation>2019-03-27T00:52:08Z</creation></dates><accession>S-EPMC3323023</accession><cross_references><pubmed>22315231</pubmed><doi>10.1074/jbc.M111.320184</doi><doi>10.1074/jbc.m111.320184</doi></cross_references></HashMap>