Protein chemical characterization of Mucor pusillus aspartic proteinase Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment

FEBS Letters

Foundling, Stephen³  Blundell, Tom¹  Pavlík, Manfred²  Baudys̆, Miroslav²  Kostka, Vladimír² 

[1] Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, England;Institute of Organic Chemistry and Bio-chemistry, Czechoslovak Academy of Sciences, Flemingovo nam. 2, CS-166 10 Prague, Czechoslovakia;E.I du Pont de Nemours & Co., Ltd, Central Research & Development Department, Bldg 328, Rm 350A, Wilmington, DE 19898, USA

关键词: Aspartic proteinase;    Amino acid sequence;    N-Glycosylation;    Disulfide bridge;    Evolution;    (Mucor pusillus);   

DOI  :  10.1016/0014-5793(88)81277-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The amino acid sequence of Mucor pusillus aspartic protenaise was determined by analysis of fragments obtained from cleavage of the enzyme by CNBr and limited tryptic digestion. The protenaise is a single polypeptide chain protein containing 361 amino acid residues, cross-linked by two disulfide bonds. A sugar moiety composed of two GlcNAc residues and four neutral sugar residues is asparagine-linked to the chain. The sequence of M. pusillus proteinase is highly homologous with the M. miehei protonaise (83% identity). The homology with other aspartic proteinases is low (22–24%) and indicates that the Mucor proteinases diverged at an early evolutionary phase. The most conservative regions of the molecule are those involved in catalysis and forming the binding cleft and the core region of the molecule.

【 授权许可】

Unknown