{"refrec":{"BRefID":281026,"RR":"<b>Claverie, P.; Vigano, C.; Ruysschaert, J.-M.; Gerday, C.; Feller, G.</b> (2003). The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation. <i>Biochimica et Biophysica Acta-Proteins and Proteomics 1649(2)</i>: 119-122. <a href=\"https://dx.doi.org/10.1016/S1570-9639(03)00184-5\" target=\"_blank\">https://dx.doi.org/10.1016/S1570-9639(03)00184-5</a>","BEntID":273045,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Biochimica et Biophysica Acta-Proteins and Proteomics 1649(2)</i>: 119-122. <a href=\"https://dx.doi.org/10.1016/S1570-9639(03)00184-5\" target=\"_blank\">https://dx.doi.org/10.1016/S1570-9639(03)00184-5</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Claverie, P.; Vigano, C.; Ruysschaert, J.-M.; Gerday, C.; Feller, G.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Claverie, P. <i>et al.</i>","Englishabstract":"The α-amylase precursor from the bacterium <i>Pseudoalteromonas haloplanktis</i> possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted β-barrel of autotransporters, this C-terminal propeptide displays a noticeable α-helix content. It is connected to the enzyme by a disordered linker and has no significant interaction with the catalytic domain. 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