Stabilisation of cathepsin E by ATP

FEBS Letters

Ueno, E.³  Thomas, D.J.²  Yamamoto, K.³  Jupp, R.A.²  Dunn, B.M.⁴  Kay, J.²  Samloff, I.M.¹  Richards, A.D.² 

[1] V.A. Medical Center, Sepulveda, CA 91343 USA;Department of Biochemistry, University College, PO Box 78, Cardiff CF1 1XL, Wales UK;Department of Pharmacology, Nagasaki University School of Dentistry, Nagasaki 852, Japan;Department of Biochemistry and Molecular Biology, J. Hillis Miller Health Center, University of Florida, Gainesville, FL 32610, USA

关键词: Cathepsin E;    Slow moving proteinase;    Erythrocyte membrane aspartic proteinase;    ATP-stimulation;    (Human);    SMP;    slow moving proteinase;    EMAP;    erythrocyte membrane aspartic proteinase;    Nph;    nitrophenylalanine;   

DOI  :  10.1016/0014-5793(89)80117-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The hydrolysis of 3 distinct substrates by cathepsin E from human red blood cells and gastric mucosa was measured in the presence and absence of physiologically relevant concentrations of ATP. At pH values below about 5.0, the nucleotide was without effect. However, at pH 5.8, whereas cathepsin E was virtually inactive by itself, it was restored to full activity (k _cat) by ATP and the non-hydrolysable methylene-ATP analogue. At still higher pH values, k _cat progressively diminished but significant levels of cathepsin E activity were readily detectable at pH 7.0. The specificity of this stabilisation effect was examined.

【 授权许可】

Unknown