{"refrec":{"BRefID":281022,"RR":"<b>Xu, Y.; Feller, G.; Gerday, C.; Glansdorff, N.</b> (2003). <i>Moritella</i> cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature? <i>J. Bacteriol. 185(18)</i>: 5519-5526. <a href=\"http://dx.doi.org/10.1128/JB.185.18.5519-5526.2003\" target=\"_blank\">dx.doi.org/10.1128/JB.185.18.5519-5526.2003</a>","BEntID":273041,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":" <i>J. Bacteriol. 185(18)</i>: 5519-5526. <a href=\"https://dx.doi.org/10.1128/JB.185.18.5519-5526.2003\" target=\"_blank\">https://dx.doi.org/10.1128/JB.185.18.5519-5526.2003</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Xu, Y.; Feller, G.; Gerday, C.; Glansdorff, N.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Xu, Y. <i>et al.</i>","Englishabstract":"Adapting metabolic enzymes of microorganisms to low temperature environments may require a difficult compromise between velocity and affinity. We have investigated catalytic efficiency in a key metabolic enzyme (dihydrofolate reductase) of <i>Moritella profunda</i> sp. nov., a strictly psychrophilic bacterium with a maximal growth rate at 2°C or less. The enzyme is monomeric (<i>M</i><sub>r</sub> = 18,291), 55% identical to its <i>Escherichia coli</i> counterpart, and displays <i>T<sub>m</sub></i> and denaturation enthalpy changes much lower than <i>E. coli</i> and <i>Thermotoga maritima</i> homologues. Its stability curve indicates a maximum stability above the temperature range of the organism, and predicts cold denaturation below 0°C. At mesophilic temperatures the apparent <i>K<sub>m</sub></i> value for dihydrofolate is 50- to 80-fold higher than for <i>E. coli</i>, <i>Lactobacillus casei</i>, and <i>T. maritima</i> dihydrofolate reductases, whereas the apparent <i>K<sub>m</sub></i> value for NADPH, though higher, remains in the same order of magnitude. At 5°C these values are not significantly modified. The enzyme is also much less sensitive than its <i>E. coli</i> counterpart to the inhibitors methotrexate and trimethoprim. The catalytic efficiency (<i>k</i><sub>cat</sub><i>/K<sub>m</sub></i>) with respect to dihydrofolate is thus much lower than in the other three bacteria. The higher affinity for NADPH could have been maintained by selection since NADPH assists the release of the product tetrahydrofolate. Dihydrofolate reductase adaptation to low temperature thus appears to have entailed a pronounced trade-off between affinity and catalytic velocity. The kinetic features of this psychrophilic protein suggest that enzyme adaptation to low temperature may be constrained by natural limits to optimization of catalytic efficiency.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"<i>Moritella</i> cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature?","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:32:52.928458","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2003,"MonPub":null,"DateUpdate":"2016-10-24","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000185181500021","VABBcode":null,"OpenAcc":0,"DOI":"10.1128/JB.185.18.5519-5526.2003"},"refs":null,"anarec":{"AnaID":281022,"PubliDate":2003,"Pagination":"5519-5526","XtraPublOfAnaID":null,"ISBN":null,"Volume":"185","Issue":"18","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":43201,"SerRR":"Journal of Bacteriology. American Society of Microbiology: Washington DC.  ISSN 0021-9193; e-ISSN 1098-5530","StandardTitleSer":"Journal of Bacteriology","ISSN":"0021-9193","AbbrevSer":"J. 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