{"refrec":{"BRefID":337652,"RR":"<b>Pierson, E.; Wouters, J.</b> (2020). Biochemical characterization of phosphoserine phosphatase SerB2 from <i>Mycobacterium marinum</i>. <i>Biochem. Biophys. Res. Commun. 530(4)</i>: 739-744. <a href=\"https://hdl.handle.net/10.1016/j.bbrc.2020.07.017\" target=\"_blank\">https://hdl.handle.net/10.1016/j.bbrc.2020.07.017</a>","BEntID":334276,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Biochem. Biophys. Res. Commun. 530(4)</i>: 739-744. <a href=\"https://hdl.handle.net/10.1016/j.bbrc.2020.07.017\" target=\"_blank\">https://hdl.handle.net/10.1016/j.bbrc.2020.07.017</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Pierson, E.; Wouters, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Pierson, E.; Wouters, J.","Englishabstract":"SerB2 is an essential phosphoserine phosphatase (PSP) that has been shown to be involved in <em>Mycobacterium tuberculosis</em> (<em>Mtb</em>) immune evasion mechanisms, and a drug target for the development of new antitubercular agents. A highly similar (91.0%) orthologous enzyme exists in the surrogate organism <em>Mycobacterium marinum</em> (<em>Mma</em>) and could have acquired similar properties. By homology modeling, we show that the two PSPs are expected to exhibit almost identical architectures. <em>Mma</em>SerB2 folds into a homodimer formed by two intertwined subunits including two ACT regulatory domains followed by a catalytic core typical of HAD (haloacid dehalogenase) phosphatases. Their <em>in vitro</em> catalytic properties are closely related as <em>Mma</em>SerB2 also depends on Mg<sup>2+</sup> for the dephosphorylation of its substrate, <em>O</em>-phospho-<span class=\"small-caps\">l</span>-serine (PS), and is most active at neutral pH and temperatures around 40 °C. Moreover, an enzyme kinetics study revealed that the enzyme is inhibited by PS as well, but at lower concentrations than <em>Mtb</em>SerB2. Substrate inhibition could occur through the binding of PS in the second active site and/or at the ACT domains interface. Finally, previously described beta-carboline <em>Mtb</em>SerB2 inhibitors also decrease the phosphatase activity of <em>Mma</em>SerB2. Altogether, these results provide useful information when <em>M.marinum</em> is used as a model to study immune evasion in tuberculosis.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Biochemical characterization of phosphoserine phosphatase SerB2 from <i>Mycobacterium marinum</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-17 01:32:39.056734","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Mycobacterium marinum; SerB2; Phosphoserine phosphatase; HADphosphatases; Clofazimine; Harmine derivatives","OtherDescriptors":null,"Notes":null,"AnaPub":2020,"MonPub":null,"DateUpdate":"2021-09-08","DateCreate":"2021-05-17","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000565646300019","VABBcode":null,"OpenAcc":0,"Handle":"10.1016/j.bbrc.2020.07.017"},"refs":null,"anarec":{"AnaID":337652,"PubliDate":2020,"Pagination":"739-744","XtraPublOfAnaID":null,"ISBN":null,"Volume":"530","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42249,"SerRR":"Biochemical and Biophysical Research Communications. 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