Characterization of Moraxella bovis Aspartate Transcarbamoylase

Characterization of Moraxella bovis Aspartate Transcarbamoylase

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 o...

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Bibliographic Details
Main Author: Hooshdaran, Sahar
Other Authors: Farinha, Mark A.
Format: Others
Language:English
Published: University of North Texas 2001
Subjects:
Pyrimidine nucleotides > Metabolism.
Moraxella.
Moraxella bovis
ATCase (aspartate tanscarbamoylase)
nucleotide effectors
growth curve
growth conditions
Online Access:https://digital.library.unt.edu/ark:/67531/metadc3012/
Description
Summary: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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