Free glycine accelerates the autoproteolytic activation of human asparaginase.
Free glycine accelerates the autoproteolytic activation of human asparaginase.
复制标题
游离甘氨酸加速了人天冬酰胺酶的自传溶解活化。
DOI：
10.1016/j.chembiol.2013.03.006
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发表时间：
2013-04-18
影响因子：
--
通讯作者：
Lavie A
中科院分区：
文献类型：
--
作者：
Su Y;Karamitros CS;Nomme J;McSorley T;Konrad M;Lavie A
Human asparaginase 3 (hASNase3), which belongs to the N-terminal nucleophile (Ntn) 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 post-translational processing, and explain why no other amino acid can substitute for glycine.
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DOI：
10.1126/science.1177585
发表时间：
2009-11-06
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Wolan DW;Zorn JA;Gray DC;Wells JA
通讯作者：
Wells JA
影响因子：
64.5
作者：
Xu, QA;Buckley, D;Guo, HC
通讯作者：
Guo, HC
DOI：
10.1111/j.1432-1033.2004.04254.x
发表时间：
2004-08-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Borek, D;Michalska, K;Jaskolski, M
通讯作者：
Jaskolski, M
apo 和产物结合的人 L-天冬酰胺酶的结构：深入了解自蛋白水解和底物水解的机制。
影响因子：
2.9
作者：
Nomme J;Su Y;Konrad M;Lavie A
通讯作者：
Lavie A
影响因子：
4.8
作者：
Michalska, Karolina;Hernandez-Santoyo, Alejandra;Jaskolski, Mariusz
通讯作者：
Jaskolski, Mariusz