7CBU
Blasnase-T13A with L-Asp
Summary for 7CBU
| Entry DOI | 10.2210/pdb7cbu/pdb |
| Descriptor | L-asparaginase, MAGNESIUM ION, FORMIC ACID, ... (5 entities in total) |
| Functional Keywords | substrate, complex, mutant, hydrolase |
| Biological source | Bacillus paralicheniformis |
| Total number of polymer chains | 2 |
| Total formula weight | 83435.82 |
| Authors | |
| Primary citation | Ran, T.,Jiao, L.,Wang, W.,Chen, J.,Chi, H.,Lu, Z.,Zhang, C.,Xu, D.,Lu, F. Structures of l-asparaginase from Bacillus licheniformis Reveal an Essential Residue for its Substrate Stereoselectivity. J.Agric.Food Chem., 69:223-231, 2021 Cited by PubMed Abstract: l-Asparaginase, which catalyzes the hydrolysis of l-asparagine, is an important enzyme in both the clinical and food industry. Exploration of efficient l-asparaginase with high substrate specificity, especially high chiral selectivity, is essential for extending its use. Herein, various crystal structures of type I l-asparaginase from (BlAsnase) have been resolved, and we found that there are two additional tyrosines in BlAsnase, contributing to the binding and catalysis of d-asparagine. Strikingly, the substitution of Tyr278 with methionine impaired the interaction with d-asparagine via water molecules due to the small hydrophobic side chain of methionine, which forced the ligand to the deep side of the active site toward the catalytic residues and thus resulted in the loss of hydrolyzing function. Our investigation of the substrate recognition mechanism of BlAsnase is significant for both a better understanding of l-asparaginase and its rational design to achieve high specificity for clinical and industrial applications. PubMed: 33371681DOI: 10.1021/acs.jafc.0c06609 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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