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Literature DB >> 4672673

The specificity of dipeptidyl aminopeptidase I (cathepsin C) and its use in peptide sequence studies.

Abstract

1. The characterization of cathepsin C as an aminodipeptidase has been confirmed. 2. An extra limitation on its specificity, namely that peptides involving proline as the third residue are immune to the enzyme, has been found. 3. A novel technique of using the enzyme for amino acid sequence determination has been shown to be feasible.

Entities: Chemical Gene

Mesh：

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Year: 1972 PMID： 4672673 PMCID： PMC1178426 DOI： 10.1042/bj1260683

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

4 in total

1. New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones.

Authors: J K McDonald; B B Zeitman; T J Reilly; S Ellis
Journal: J Biol Chem Date: 1969-05-25 Impact factor: 5.157

2. A theoretical investigation into the potential usefulness of the cathepsin C 'domino' technique.

Authors: R J Rowlands; H Lindley
Journal: Biochem J Date: 1972-02 Impact factor: 3.857

3. Human fibrinopeptides. Isolation, characterization and structure.

Authors: B Blombäck; M Blombäck; P Edman; B Hessel
Journal: Biochim Biophys Acta Date: 1966-02-28

4. Purification and properties of dipeptidyl transferase (Cathepsin C).

Authors: R M Metroione; A G Neves; J S Fruton
Journal: Biochemistry Date: 1966-05 Impact factor: 3.162

4 in total

1. Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I).

Authors: Martin Horn; Miroslav Baudys; Zdenek Voburka; Ivan Kluh; Jirí Vondrásek; Michael Mares
Journal: Protein Sci Date: 2002-04 Impact factor: 6.725

The specificity of dipeptidyl aminopeptidase I (cathepsin C) and its use in peptide sequence studies.

1. New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones.

2. A theoretical investigation into the potential usefulness of the cathepsin C 'domino' technique.

3. Human fibrinopeptides. Isolation, characterization and structure.

4. Purification and properties of dipeptidyl transferase (Cathepsin C).

1. Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I).

2. A theoretical investigation into the potential usefulness of the cathepsin C 'domino' technique.

3. A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism.

4. Synthesis of dehydrodipeptide esters and their evaluation as inhibitors of cathepsin C.