The primary structure of carboxypeptidase S1 from Penicillium janthinellum.
The complete amino acid sequence of carboxypeptidase S1 from Penicillium janthinellium has been determined by N-terminal sequencing of the reduced and vinylpyridinated protein and of peptides obtained by cleaved 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.
Svendsen
I
I
Carlsberg Laboratory, Department of Chemistry, Copenhagen, Denmark.
Hofmann
T
T
Endrizzi
J
J
Remington
S J
SJ
Breddam
K
K
D000595:Amino Acid Sequence; D001665:Binding Sites; D002268:Carboxypeptidases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D002268:Carboxypeptidases; C022326:penicillocarboxypeptidase-S