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Carbamyl phosphate synthesis in Nuerospora crassa I. Preliminary characterization of arginine-specific carbamyl phosphokinase
dc.contributor.authorDavis, Rowland H.en_US
dc.date.accessioned2006-04-13T14:41:10Z
dc.date.available2006-04-13T14:41:10Z
dc.date.issued1965-08-24en_US
dc.identifier.citationDavis, Rowland H. (1965/08/24)."Carbamyl phosphate synthesis in Nuerospora crassa I. Preliminary characterization of arginine-specific carbamyl phosphokinase." Biochimica et Biophysica Acta (BBA) - General Subjects 107(1): 44-53. <http://hdl.handle.net/2027.42/31986>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1W-47NWJVF-H3/2/e24b55792473b76cff6e14ba2f2c2bc9en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/31986
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5857367&dopt=citationen_US
dc.description.abstractAn enzyme from Neurospora crassa which catalyzes carbamyl phosphate formation is reported. Carbamyl phosphate formation by the enzyme is hown to be dependent upon ATP, ammonia, bicarbonate, and magnesium ions. Glutamine and , involved in carbamyl phosphate synthesis in other organisms, are not required for the reaction and do not influence it. While direct evidence for cabamate as the substrate is lacking, the enzyme is considered to bacterial carbamyl phosphokinase (ATP : carbanate phosphotransferease, EC 2.7.2.2).en_US
dc.format.extent751351 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleCarbamyl phosphate synthesis in Nuerospora crassa I. Preliminary characterization of arginine-specific carbamyl phosphokinaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Botany, University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.identifier.pmid5857367en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/31986/1/0000028.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0304-4165(65)90387-9en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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