8ECE
E. coli L-asparaginase II mutant (V27T) in complex with L-Glu
Summary for 8ECE
| Entry DOI | 10.2210/pdb8ece/pdb |
| Descriptor | L-asparaginase 2, GLUTAMIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | hydrolase, hydrolysis of l-asparagine |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 4 |
| Total formula weight | 143714.61 |
| Authors | Strzelczyk, P.,Wlodawer, A.,Lubkowski, J. (deposition date: 2022-09-01, release date: 2022-11-16, Last modification date: 2024-11-06) |
| Primary citation | Strzelczyk, P.,Zhang, D.,Wlodawer, A.,Lubkowski, J. The E. coli L-asparaginase V27T mutant: structural and functional characterization and comparison with theoretical predictions. Febs Lett., 596:3060-3068, 2022 Cited by PubMed Abstract: Bacterial L-asparaginases have been used for over 40 years as anticancer drugs. Ardalan et al. (Medical Hypotheses 112, 7-17, 2018) proposed that the V27T mutant of Escherichia coli type II L-asparaginase, EcAII(V27T), should display altered biophysical and catalytic properties compared to the wild-type enzyme, EcAII(wt), rendering it more favourable as a pharmaceutical. They postulated that EcAII(V27T) would exhibit reduced glutaminolytic activity and be more stable compared to EcAII(wt). Their postulates, however, were purely theoretical. Here, we characterized experimentally selected properties of EcAII(V27T). We found asparaginolytic activity of this mutant unchanged, whereas its glutaminolytic activity was fourfold lower compared with EcAII(wt). We did not observe significant differences in stabilities of EcAII(wt) and EcAII(V27T). Crystal structures of the complexes with L-Asp and L-Glu showed considerable differences in binding modes of both substrates. PubMed: 36310372DOI: 10.1002/1873-3468.14526 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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