Bovine inositol monophosphatase: proteolysis and structural studies

FEBS Letters

Gore, M.G.¹  Greasley, P.J.¹  Ragan, C.I.²  Rees-Milton, K.J.¹ 

[1] Dept. of Biochemistry, Centre of Molecular Recognition, School of Biological Sciences, University of Southampton. Bassett Crescent East, Southampton, S09 3TU, UK;Neurosciences Research Centre, Merck Sharp and Dohme. Terlings Park, Eastwick Road, Harlow, Essex, CM20 2QR, UK

关键词: Inositol monophosphatase;    Proteolysis;    Protein structure;    Circular dichroism;   

DOI  :  10.1016/0014-5793(93)80035-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bovine brain inositol monophosphatase is inactivated when trypsin catalyses the cleavage of a single peptide bond between Lys-36 and Ser-37. This proteolysis is closely followed by cleavage at two other sites in the protein between Lys-78 and Ser-79 and between Lys-156 and Ser-157 suggesting that all of these sites are exposed in the native conformation of the protein. All of these residues are predicted to lie at the ends of α helices. The most susceptible bond (Lys-36-Ser-37) is predicted to lie in a highly flexible region of the protein. Circular dichroism studies suggest that approximately 40% of the secondary structure of this protein is helical which is similar to that predicted by the algorithm of Gamier et al. [(1978) J. Mol. Biol. 120, 97-120].

【 授权许可】

Unknown