Intramolecular Cleavage of the hASRGL1 Homodimer Occurs in Two Stages.
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Li W, Irani S, Crutchfield A, Hodge K, Matthews W, Patel P, Zhang YJ, Stone E
Intramolecular Cleavage of the hASRGL1 Homodimer Occurs in Two Stages.
Biochemistry. 2016 Feb 16;55(6):960-9. doi: 10.1021/acs.biochem.5b01157. Epub 2016 Feb 2.
- PubMed ID
- 26780688 [ View in PubMed]
- Abstract
The human asparaginase-like protein 1 (hASRGL1) is a member of the N-terminal nucleophile (Ntn) family that hydrolyzes l-asparagine and isoaspartyl-dipeptides. The nascent protein folds into an alphabeta-betaalpha sandwich fold homodimer that cleaves its own peptide backbone at the G167-T168 bond, resulting in the active form of the enzyme. However, biophysical studies of hASRGL1 are difficult because of the curious fact that intramolecular cleavage of the G167-T168 peptide bond reaches only
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Asparagine Isoaspartyl peptidase/L-asparaginase Protein Humans NoSubstrateDetails