The primary structure of carboxypeptidase S1 from Penicillium janthinellum
- 25 October 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 333 (1-2) , 39-43
- https://doi.org/10.1016/0014-5793(93)80371-z
Abstract
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.Keywords
This publication has 20 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Refined atomic model of wheat serine carboxypeptidase II at 2.2-.ANG. resolutionBiochemistry, 1992
- Structural determination of the essential serine and glycosylation sites of carboxypeptidase PArchives of Biochemistry and Biophysics, 1992
- The primary structure of the glutamic acid‐specific protease ofStreptomyces griseusFEBS Letters, 1991
- Primary structure of carboxypeptidase III from malted barleyCarlsberg Research Communications, 1989
- Purification and amino acid sequence determination of an endo-1,3-β-glucanase from barleyCarlsberg Research Communications, 1988
- Carboxypeptidase S-1 from Penicillium janthinellum: Enzymatic properties in hydrolysis and aminolysis reactionsCarlsberg Research Communications, 1988
- Chemical modifications of a cysteinyl residue introduced in the binding site of carboxypeptidase Y by site-directed mutagenesisCarlsberg Research Communications, 1988
- Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptideCell, 1987
- Modification of the single sulfhydryl group of carboxypeptidase Y with mercurials. Influence on enzyme specificityCarlsberg Research Communications, 1983