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The primary structure of carboxypeptidase S1 from Penicillium janthinellum
Author(s) -
Svendsen Ib,
Hofmann Theo,
Endrizzi Jim,
Remington S.James,
Breddam Klaus
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80371-z
Subject(s) - carboxypeptidase , chemistry , microbiology and biotechnology , biology , biochemistry , enzyme
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.