Characterization of Moraxella bovis Aspartate Transcarbamoylase

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Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious organism, the etiologic agent of infectious bovine keratoconjunctivitis (IBK). The M. bovis ATCase was purified and characterized for the first time. It is a class A enzyme with a molecular mass of 480 to 520 kDa. It has a pH optimum of 9.5 and is stable at high temperatures. The ATCase holoenzyme is inhibited by CTP > ATP > ... continued below

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Hooshdaran, Sahar December 2001.

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  • Hooshdaran, Sahar

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Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious organism, the etiologic agent of infectious bovine keratoconjunctivitis (IBK). The M. bovis ATCase was purified and characterized for the first time. It is a class A enzyme with a molecular mass of 480 to 520 kDa. It has a pH optimum of 9.5 and is stable at high temperatures. The ATCase holoenzyme is inhibited by CTP > ATP > UTP. The Km for aspartate is 1.8 mM and the Vmax 1.04 µmol per min, where the Km for carbamoylphosphate is 1.05 mM and the Vmax 1.74 µmol per min.

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  • December 2001

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  • Sept. 25, 2007, 10:40 p.m.

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  • Nov. 26, 2008, 3:46 p.m.

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Hooshdaran, Sahar. Characterization of Moraxella bovis Aspartate Transcarbamoylase, thesis, December 2001; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc3012/: accessed September 25, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .