8ecd | pdb_00008ecd

E. coli L-asparaginase II mutant (V27T) in complex with L-Asp

spinqualitylabelsall models 8ecd, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ecd is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.62Å Ligands: ASP, CIT, EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ASPG2_ECOLI Publication Abstract from PubMed 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. The E. coli L-asparaginase V27T mutant: structural and functional characterization and comparison with theoretical predictions.,Strzelczyk P, Zhang D, Wlodawer A, Lubkowski J FEBS Lett. 2022 Oct 30. doi: 10.1002/1873-3468.14526. PMID:36310372 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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