{"refrec":{"BRefID":261824,"RR":"<b>Xu, Y.; Zhang, Y.; Liang, Z.; Van de Casteele, M.; Legrain, C.; Glansdorff, N.</b> (1998). Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, <i>Vibrio</i> strain 2693: properties of the enzyme, genetic organization and synthesis in <i>Escherichia coli</i>. <i>Microbiology 144</i>: 1435-1441. <a href=\"http://dx.doi.org/10.1099/00221287-144-5-1435\" target=\"_blank\">http://dx.doi.org/10.1099/00221287-144-5-1435</a>","BEntID":253842,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Microbiology 144</i>: 1435-1441. <a href=\"http://dx.doi.org/10.1099/00221287-144-5-1435\" target=\"_blank\">http://dx.doi.org/10.1099/00221287-144-5-1435</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Xu, Y.; Zhang, Y.; Liang, Z.; Van de Casteele, M.; Legrain, C.; Glansdorff, N.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Xu, Y. <i>et al.</i>","Englishabstract":"The aspartate carbamoyltransferase (ATCase) genes of psychrophilic <i>Vibrio</i> strain 2693 were cloned by complementation in <i>Escherichia coli</i> and the enzyme was partly characterized. The genes constitute a <i>pyrBl</i> operon homologous to the cognate structure in <i>E. coli</i> where <i>pyrB</i> and <i>pyrl</i> respectively encode the catalytic and the regulatory chains of ATCase. The strong sequence similarities noted between <i>Vibrio</i> and <i>E. coli</i> ATCases include extensive conservation of residues involved in interactions between subunits, suggesting that the two enzymes have very similar tertiary and quaternary structures. <i>Vibrio</i> ATCase is, however, not activated by ATP and not synergistically inhibited by CTP and UTP. It is also much more thermolabile than <i>E. coli</i> ATCase. With respect to <i>Pyrococcus abyssi</i> and <i>E. coli</i> ATCases, <i>Vibrio</i> ATCase presents marked differences in composition which could be related to its psychrophilic character. The results of these structural and functional comparisons indicate that <i>Vibrio</i> 2693 ATCase is a suitable model for biochemical studies on structure-function relationships in a ‘cold’ allosteric enzyme. The operon is expressed from a promoter which is immediately followed by a pyrimidine-rich leader ORF terminating within a putative transcription attenuator. These genetic and enzymic data strengthen the evolutionary relationship already noted between Vibrionaceae and Enterobacteriaceae.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, <i>Vibrio</i> strain 2693: properties of the enzyme, genetic organization and synthesis in <i>Escherichia coli</i>","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":"aspartate carbamoyltransferase; psychrophiles; Vibrio","OtherDescriptors":null,"Notes":null,"AnaPub":1998,"MonPub":null,"DateUpdate":"2016-10-28","DateCreate":"2016-10-03","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000073681800033","VABBcode":null,"OpenAcc":1,"DOI":"10.1099/00221287-144-5-1435"},"refs":null,"anarec":{"AnaID":261824,"PubliDate":1998,"Pagination":"1435-1441","XtraPublOfAnaID":null,"ISBN":null,"Volume":"144","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":43402,"SerRR":"Microbiology. 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