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- W3173590136 endingPage "531" @default.
- W3173590136 startingPage "514" @default.
- W3173590136 abstract "L-Asparaginases have remained an intriguing research topic since their discovery ∼120 years ago, especially after their introduction in the 1960s as very efficient antileukemic drugs. In addition to bacterial asparaginases, which are still used to treat childhood leukemia, enzymes of plant and mammalian origin are now also known. They have all been structurally characterized by crystallography, in some cases at outstanding resolution. The structural data have also shed light on the mechanistic details of these deceptively simple enzymes. Yet, despite all this progress, no better therapeutic agents have been found to beat bacterial asparaginases. However, a new option might arise with the discovery of yet another type of asparaginase, those from symbiotic nitrogen-fixing Rhizobia, and with progress in the protein engineering of enzymes with desired properties. This review surveys the field of structural biology of L-asparaginases, focusing on the mechanistic aspects of the well established types and speculating about the potential of the new members of this amazingly diversified family." @default.
- W3173590136 created "2021-07-05" @default.
- W3173590136 creator A5004093880 @default.
- W3173590136 creator A5051513752 @default.
- W3173590136 date "2021-06-30" @default.
- W3173590136 modified "2023-10-15" @default.
- W3173590136 title "Structural and biophysical aspects of <scp>L</scp>-asparaginases: a growing family with amazing diversity" @default.
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