5I8I
Crystal Structure of the K. lactis Urea Amidolyase
Summary for 5I8I
| Entry DOI | 10.2210/pdb5i8i/pdb |
| Related | 3VA7 4ISS |
| Descriptor | Urea Amidolyase (1 entity in total) |
| Functional Keywords | hyrolase, biotin-dependent carboxylase, hydrolase |
| Biological source | Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 808105.94 |
| Authors | |
| Primary citation | Zhao, J.,Zhu, L.,Fan, C.,Wu, Y.,Xiang, S. Structure and function of urea amidolyase. Biosci. Rep., 38:-, 2018 Cited by PubMed Abstract: Urea is the degradation product of a wide range of nitrogen containing bio-molecules. Urea amidolyase (UA) catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source. It is widely distributed in fungi, bacteria and other microorganisms, and plays an important role in nitrogen recycling in the biosphere. UA is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains, which catalyze sequential reactions. In some organisms UC and AH are encoded by separated genes. We present here structure of the (KlUA). The structure revealed that KlUA forms a compact homo-dimer with a molecular weight of 400 kDa. Structure inspired biochemical experiments revealed the mechanism of its reaction intermediate translocation, and that the KlUA holo-enzyme formation is essential for its optimal activity. Interestingly, previous studies and ours suggest that UC and AH encoded by separated genes probably do not form a KlUA-like complex, consequently they might not catalyze the urea to ammonium conversion as efficiently. PubMed: 29263142DOI: 10.1042/BSR20171617 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6.5 Å) |
Structure validation
Download full validation report
