Characterization of Aspartate Transcarbamoylase in the Archaebacterium Methanococcus Jannaschii
Description:
Asparate transcarbamoylase catalyzes the first committed step in the de novo synthesis of pyrmidine nucleotides UMP, UDP, UTP, and CTP. The archetype enzyme found in Escherichia coli (310 kDa) exhibits sigmodial substrate binding kinetics with positive control by ATP and negative control with CTP and UTP. The ATCase characterized in this study is from the extreme thermophilic Archaebacterium, Methanococcus jannaschii. The enzyme was very stable at elevated temperatures and possessed activity fr…
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Date:
December 1996
Creator:
Stewart, John E. B. (John Edward Bakos)
Partner:
UNT Libraries