The primary structure of carboxypeptidase S1 from Penicillium janthinellum

FEBS Letters

Endrizzi, Jim³  Svendsen, Ib¹  Hofmann, Theo²  Breddam, Klaus¹  Remington, S.James³ 

[1] Carlsberg Laboratory, Department of Chemistry, Garnie Carlsberg Vej 10, DK-2500 Copenhagen, Denmark;Department of Biochemistry, University of Toronto, Toronto, Ont. M5S lA8, Canada;University of Oregon, Institute of Molecular Biology, Eugene, OR 97403-1229, USA

关键词: Carboxypeptidase;    Serine protease;    Amino acid sequence;    CPD-S1;    carboxypeptidase S1 (from P. janthinellum);    CPD-Y;    carboxypeptidase Y (from yeast);    CPD-MIII;    carboxypeptidase MIII (from barley malt);    CPDW-II;    carboxypeptidase II from wheat;    CNBr;    cyanogen bromide. The binding site notation is that of Schechter and Berger [1];   

DOI  :  10.1016/0014-5793(93)80371-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of carboxypeptidase Sl from Penicillium janthinellum has been determined by N-terminal sequencing of the reduced and vinylpyridinated protein and of peptides obtained by cleavage with cyanogen bromide, iodosobenzoic acid, hydroxylamine, endoproteinase LysC, endoproteinase AspN and Glu-specific proteinase from B. licheniformis. The enzyme consists of a single peptide chain of 433 amino acid residues and contains 9 half-cystine residues and one glycosylated asparagine residue. A comparison to other carboxypeptidases shows that the enzyme is homologous to carboxypeptidase-Y and carboxypeptidase-MIII from malt. Specificity and binding of substrates are discussed from a three-dimensional model based on the known structure of carboxypeptidase-Y from Saccharomyces cereviciae and carboxypeptidase II from wheat.

【 授权许可】

Unknown