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  Free glycine accelerates the autoproteolytic activation of human asparaginase.

Su, Y., Karamitros, C. S., Nomme, J., McSorley, T., Konrad, M., & Lavie, A. (2013). Free glycine accelerates the autoproteolytic activation of human asparaginase. Chemistry and Biology, 20(4), 533-540. doi:10.1016/j.chembiol.2013.03.006.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-7639-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-5D26-F
Genre: Journal Article

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Su, Y., Author
Karamitros, C. S.1, Author              
Nomme, J., Author
McSorley, T.1, Author              
Konrad, M.1, Author              
Lavie, A., Author
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1Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              

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 Abstract: 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 glycine selectively acts to accelerate hASNase3 cleavage both in vitro and in human cells. Other small amino acids such as alanine, serine, or the substrate asparagine are not capable of promoting autoproteolysis. Crystal structures of hASNase3 in complex with glycine in the uncleaved and cleaved enzyme states reveal the mechanism of glycine-accelerated posttranslational processing and explain why no other amino acid can substitute for glycine.

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Language(s): eng - English
 Dates: 2013-04-18
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.chembiol.2013.03.006
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Title: Chemistry and Biology
Source Genre: Journal
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Pages: - Volume / Issue: 20 (4) Sequence Number: - Start / End Page: 533 - 540 Identifier: -