Three-dimensional structure and mechanism of urea hydrolase

Recently, the Journal of Biological Chemistry published the research paper of Structure and function of allophanate hydrolase by Xiang Song Research Group, Institute of Nutritional Sciences, Chinese Academy of Sciences and Shanghai Institutes for Biological Sciences. This study parsed the three-dimensional structure of allophanate hydrolase (AH) and revealed the mechanism of its catalytic reaction.

AH is distributed in various microorganisms and catalyzes the conversion of allophanate to ammonia. AH and urea carboxylase (UC) form a urea amidolyase (UA) complex, which catalyzes the conversion of urea to ammonia. It is an important link for many microorganisms to use urea as a nitrogen source for their metabolism. Urea is a metabolite of various nitrogen-containing biomolecules. Using it as a nitrogen source is an important part of the cycle of nitrogen in the life cycle. However, the three-dimensional structure of AH and its specific role in urea (allophanate) catalysis to ammonia The mechanism is unclear.

On the basis of revealing the structure of UC and the catalytic reaction mechanism in the early stage, Fan Chen, a doctoral student under the guidance of Prof. Song Song, conducted a cooperative research with Yin Huiyong Group of the Institute of Nutrition and analyzed the crystal structure of AH using crystallography. The results show that: AH is composed of two catalytic domains, respectively participating in one step of the two-step catalytic reaction, and reveals the catalytic mechanism of each step. Interestingly, the study found that one step reaction may represent a novel decarboxylation reaction. This work not only promoted people's understanding of the functional mechanism of UA and microbial absorption of urea as a nitrogen source, but also expanded the understanding of biological decarboxylation reactions.

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

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