4ISS
SeMet-substituted Kluyveromyces lactis Allophanate Hydrolase
Summary for 4ISS
| Entry DOI | 10.2210/pdb4iss/pdb |
| Related | 4IST |
| Descriptor | Allophanate Hydrolase, D(-)-TARTARIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | mixed alpha and beta structure, allophanate binding, hydrolase |
| Biological source | Kluyveromyces lactis (Yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 141921.92 |
| Authors | |
| Primary citation | Fan, C.,Li, Z.,Yin, H.,Xiang, S. Structure and function of allophanate hydrolase. J.Biol.Chem., 288:21422-21432, 2013 Cited by PubMed Abstract: Allophanate hydrolase converts allophanate to ammonium and carbon dioxide. It is conserved in many organisms and is essential for their utilization of urea as a nitrogen source. It also has important functions in a newly discovered eukaryotic pyrimidine nucleic acid precursor degradation pathway, the yeast-hypha transition that several pathogens utilize to escape the host defense, and an s-triazine herbicide degradation pathway recently emerged in many soil bacteria. We have determined the crystal structure of the Kluyveromyces lactis allophanate hydrolase. Together with structure-directed functional studies, we demonstrate that its N and C domains catalyze a two-step reaction and contribute to maintaining a dimeric form of the enzyme required for their optimal activities. Our studies also provide molecular insights into their catalytic mechanism. Interestingly, we found that the C domain probably catalyzes a novel form of decarboxylation reaction that might expand the knowledge of this common reaction in biological systems. PubMed: 23754281DOI: 10.1074/jbc.M113.453837 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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