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Urea carboxylase (UC) is conserved in many bacteria, algae, and fungi and catalyzes the conversion of urea to allophanate, an essential step in the utilization of urea as a nitrogen source in these organisms.UC belongs to the biotin-dependent carboxylase superfamily and shares the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains with these other enzymes, but its carboxyltransferase (CT) domain is distinct.Structural and sequence analysis indicate that its CT domain belongs to a large family of proteins with diverse functions, including the Kip A-Kip I complex, which has important regulatory functions in the sporulation (21).A structure of the Kip A-Kip I complex is not currently available, and the UC structure provides a framework to understand the function of this complex.Currently, there is no information on the molecular basis of catalysis by UC.We report here the crystal structure of the UC and biochemical studies to assess the structural information.For example, the site cannot determine your email name unless you choose to type it.
In general, only the information that you provide, or the choices you make while visiting a web site, can be stored in a cookie.The BC and BCCP domains of biotin-dependent carboxylases are highly homologous, but their CT domains are distinct.Recently, high resolution crystal structures of the PC (18, 19) and PCC (20) holoenzymes have been reported, which greatly advanced the understanding of biotin-dependent carboxylases.In agriculture, urea is widely used as a fertilizer.In the digestive tracts of many animals, the residing microbes utilize urea from the host to produce biomass, which contributes to the host's nutrient intake (1, 4).
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Urea amidolyase has been identified in fungi (9, 10), algae (11), and bacteria (5, 6); recent studies revealed that it is widely distributed in fungi and bacteria (7, 8). By adopting urea amidolyase for their urea utilization, they avoid the transition metal nickel, whose cellular level has to be tightly regulated (7).