{"refrec":{"BRefID":281092,"RR":"<b>Purcarea, C.; Hervé, G.; Cunin, R.; Evans, D.R.</b> (2001). Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from <i>Pyrococcus abyssi</i>. <i>Extremophiles 5(4)</i>: 229-239. <a href=\"https://dx.doi.org/10.1007/s007920100201\" target=\"_blank\">https://dx.doi.org/10.1007/s007920100201</a>","BEntID":273111,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Extremophiles 5(4)</i>: 229-239. <a href=\"https://dx.doi.org/10.1007/s007920100201\" target=\"_blank\">https://dx.doi.org/10.1007/s007920100201</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Purcarea, C.; Hervé, G.; Cunin, R.; Evans, D.R.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Purcarea, C. <i>et al.</i>","Englishabstract":"<i>Pyrococcus abyssi</i>, a hyperthermophilic archaeon found in the vicinity of deep-sea hydrothermal vents, grows optimally at temperatures around 100°C. Carbamoyl phosphate synthetase (CPSase) from this organism was cloned and sequenced. The active 34-kDa recombinant protein was overexpressed in<i> Escherichia coli</i> when the host cells were cotransformed with a plasmid encoding tRNA synthetases for low-frequency<i> Escherichia coli</i> codons. Sequence homology suggests that the tertiary structure of<i> P. abyssi</i> CPSase, resembling its counterpart in<i> Pyrococcus furiosus</i>, is closely related to the catabolic carbamate kinases and is very different from the larger mesophilic CPSases.<i> P. furiosus</i> CPSase and carbamate kinase form carbamoyl phosphate by phosphorylating carbamate produced spontaneously in solution from ammonia and bicarbonate. In contrast,<i> P. abyssi</i> CPSase has intrinsic bicarbonate-dependent ATPase activity, suggesting that the enzyme can catalyze the phosphorylation of the isosteric substrates carbamate and bicarbonate.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Cloning, expression, and structure analysis of carbamate kinase-like carbamoyl phosphate synthetase from <i>Pyrococcus abyssi</i>","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":"carbamate kinase; carbamoyl phosphate synthetase; Pyrococcus abyssi;evolution; archaea; hyperthermophily","OtherDescriptors":null,"Notes":null,"AnaPub":2001,"MonPub":null,"DateUpdate":"2022-05-02","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000170563600003","VABBcode":null,"OpenAcc":0,"DOI":"10.1007/s007920100201"},"refs":null,"anarec":{"AnaID":281092,"PubliDate":2001,"Pagination":"229-239","XtraPublOfAnaID":null,"ISBN":null,"Volume":"5","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":218588,"SerRR":"Extremophiles. 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