Free glycine accelerates the autoproteolytic activation of human asparaginase.
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ABSTRACT:
SUBMITTER: Su Y
PROVIDER: S-EPMC3633088 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Publications
Free glycine accelerates the autoproteolytic activation of human asparaginase.
Su Ying Y Karamitros Christos S CS Nomme Julian J McSorley Theresa T Konrad Manfred M Lavie Arnon A
Chemistry & biology 20130401 4
Human asparaginase 3 (hASNase3), which belongs to the N-terminal nucleophile hydrolase superfamily, is synthesized as a single polypeptide that is devoid of asparaginase activity. Intramolecular autoproteolytic processing releases the amino group of Thr168, a moiety required for catalyzing asparagine hydrolysis. Recombinant hASNase3 purifies as the uncleaved, asparaginase-inactive form and undergoes self-cleavage to the active form at a very slow rate. Here, we show that the free amino acid glyc ...[more]
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