https://scholars.lib.ntu.edu.tw/handle/123456789/454737
標題: | Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases | 作者: | Veeramani S. MING-SHYUE LEE Lin M.-F. |
公開日期: | 2009 | 卷: | 34 | 期: | 6 | 起(迄)頁: | 273-278 | 來源出版物: | Trends in Biochemical Sciences | 摘要: | Although classical protein tyrosine phosphatase (PTP) superfamily members are cysteine-dependent, emerging evidence shows that many acid phosphatases (AcPs) function as histidine-dependent PTPs in vivo. These AcPs dephosphorylate phospho-tyrosine substrates intracellularly and could have roles in development and disease. In contrast to cysteine-dependent PTPs, they utilize histidine, rather than cysteine, for substrate dephosphorylation. Structural analyses reveal that active site histidine, but not cysteine, faces towards the substrate and functions as the phosphate acceptor. Nonetheless, during dephosphorylation, both histidine-dependent and cysteine-dependent PTPs use their active site arginine and aspartate for substrate binding and proton donation, respectively. Thus, we propose that they should be referred to as a distinct group of 'histidine-dependent PTPs' within the PTP superfamily. ? 2009 Elsevier Ltd. All rights reserved. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-66949135016&doi=10.1016%2fj.tibs.2009.03.002&partnerID=40&md5=10854ab07314f6cdaa9d3df0dd2cff01 https://scholars.lib.ntu.edu.tw/handle/123456789/454737 |
ISSN: | 0968-0004 | DOI: | 10.1016/j.tibs.2009.03.002 | SDG/關鍵字: | acid phosphatase; arginine; aspartic acid; cysteine; epidermal growth factor receptor 2; epidermal growth factor receptor 4; histidine; membrane enzyme; protein tyrosine phosphatase; protein Wzc; unclassified drug; amino acid metabolism; amino acid sequence; article; enzyme active site; enzyme activity; enzyme binding; enzyme structure; enzyme substrate; human; in vivo study; nerve cell; nonhuman; phytochemistry; priority journal; prostate epithelium; protein dephosphorylation; protein expression; Acid Phosphatase; Animals; Catalytic Domain; Cysteine; Histidine; Humans; Models, Biological; Neurons; Phosphates; Phylogeny; Plants; Protein Conformation; Protein Tyrosine Phosphatases; Species Specificity |
顯示於: | 生物化學暨分子生物學科研究所 |
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