A mutation in the catalytic cistron of aspartate carbamoyltransferase affecting catalysis, regulatory response and holoenzyme assembly

We describe here a mutation in the gene encoding the catalytic subunit of aspartate carbamoyltransferase (ATCase, pyr B) which produces an enzyme retaining catalytic activity as holoenzyme (2C 3 :3R 2 ) and catalytic trimer (C 3 ) but which shows neither cooperative substrate kinetics nor nucleotide...

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Veröffentlicht in:	Nature (London) 1981-07, Vol.292 (5821), p.373-375
Hauptverfasser:	Wild, James R., Foltermann, Karen F., Roof, William D., O'Donovan, Gerard A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aspartate Carbamoyltransferase - genetics Aspartate Carbamoyltransferase - metabolism Escherichia coli Escherichia coli - drug effects Escherichia coli - enzymology Genes Humanities and Social Sciences Kinetics letter Macromolecular Substances multidisciplinary Mutation Science Science (multidisciplinary) Transduction, Genetic
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