Recently, the American Journal of Biological Chemistry (Journal of Biological Chemistry) published online the research paper Crystal Structure of ureacarboxylase provides insights into the carboxyltransfer reaction. This study analyzed the three-dimensional structure of urea carboxylase (urea carboxylase, UC) and revealed the mechanism of its CarboxylTransferase (CT) domain catalytic reaction.

UC belongs to the biotin-dependent carboxylase family. Members of this family can carboxylate a variety of substrate molecules and play an important role in multiple metabolic pathways. UC is distributed in a variety of microorganisms, and the conversion reaction it catalyzes to produce urea (allophanate) is an essential link for these microorganisms to obtain nitrogen, which plays an important role in the cycle of the biosphere. Fan Chen, a PhD student under the guidance of Prof. Song Song, used crystallography to analyze the crystal structure of UC, captured an intermediate state of the catalytic reaction of its CT domain, and combined with the results of functional experiments guided by structural information, revealed the CT domain The mechanism of the catalytic reaction. In addition, analysis shows that the CT structure of UC is similar to other biotin-dependent carboxylase, so understanding the structure and function of UC also helps to understand the catalytic mechanism of other members of the biotin carboxylase family.

This subject was funded by the Ministry of Science and Technology and the Chinese Academy of Sciences.

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