{"refrec":{"BRefID":257995,"RR":"<b>Huston, A.L.; Haeggstrom, J.; Feller, G.</b> (2008). Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile <i>Colwellia psychrerythraea</i> and of human leukotriene A<sub>4</sub> hydrolase. <i>Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784(11)</i>: 1865-1872. <a href=\"https://dx.doi.org/10.1016/j.bbapap.2008.06.002\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbapap.2008.06.002</a>","BEntID":250005,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784(11)</i>: 1865-1872. <a href=\"https://dx.doi.org/10.1016/j.bbapap.2008.06.002\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbapap.2008.06.002</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Huston, A.L.; Haeggstrom, J.; Feller, G.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Huston, A.L. <i>et al.</i>","Englishabstract":"The relationships between structure, activity, stability and flexibility of a cold-adapted aminopeptidase produced by a psychrophilic marine bacterium have been investigated in comparison with a mesophilic structural and functional human homolog. Differential scanning calorimetry, fluorescence monitoring of thermal- and guanidine hydrochloride-induced unfolding and fluorescence quenching were used to show that the cold-adapted enzyme is characterized by a high activity at low temperatures, a low structural stability versus thermal and chemical denaturants and a greater structural permeability to a quenching agent relative to the mesophilic homolog. These findings support the hypothesis that cold-adapted enzymes maintain their activity at low temperatures as a result of increased global or local structural flexibility, which results in low stability. Analysis of the thermodynamic parameters of irreversible thermal unfolding suggests that entropy-driven factors are responsible for the fast unfolding rate of the cold-adapted aminopeptidase. A reduced number of proline residues, a lower degree of hydrophobic residue burial and a decreased surface accessibility of charged residues may be responsible for this effect. On the other hand, the reduction in enthalpy-driven interactions is the primary determinant of the weak conformational stability.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile <i>Colwellia psychrerythraea</i> and of human leukotriene A<sub>4</sub> hydrolase","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Psychrophile; Cold-active enzyme; Aminopeptidase; Colwelliapsychrerythraea; Leukotriene A(4) hydrolase","OtherDescriptors":null,"Notes":null,"AnaPub":2008,"MonPub":null,"DateUpdate":"2019-06-26","DateCreate":"2016-05-29","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000261019000048","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.bbapap.2008.06.002"},"refs":null,"anarec":{"AnaID":257995,"PubliDate":2008,"Pagination":"1865-1872","XtraPublOfAnaID":null,"ISBN":null,"Volume":"1784","Issue":"11","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":258648,"SerRR":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 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