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 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.

Grantor dc:publisher

University of North Texas

Year dc:date

2001

Author dc:creator

• Hooshdaran, Sahar

Contributors dc:contributor

• Farinha, Mark A.
• O'Donovan, Gerard A.
• Benjamin, Robert C.

• Pyrimidine nucleotides -- Metabolism.
• Moraxella.
• Moraxella bovis
• ATCase
• nucleotide effectors
• growth curve
• growth conditions

Statement dc:rights

• Use restricted to UNT Community
• Copyright
• Hooshdaran, Sahar
• Copyright is held by the author, unless otherwise noted. All rights reserved.

Language dc:language

English

Identifier

oclc: 51986132
https://digital.library.unt.edu/ark:/67531/metadc3012/
ark: ark:/67531/metadc3012

OAI identifier oai:identifier

info:ark/67531/metadc3012