Proline-Dependent Structural and Biological Properties of Peptides and Proteins
| Autor: | Arieh Yaron, Fred Naider, S. Scharpe |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Proline
Protein Conformation medicine.medical_treatment Molecular Sequence Data Peptide Biochemistry Dipeptidyl peptidase Prolyl endopeptidase HIV-1 protease medicine Animals Humans Peptide bond Amino Acid Sequence Molecular Biology Protein secondary structure chemistry.chemical_classification Protease biology Proteins chemistry biology.protein Peptides Peptide Hydrolases medicine.drug |
| Zdroj: | Critical Reviews in Biochemistry and Molecular Biology. 28:31-81 |
| ISSN: | 1549-7798 1040-9238 |
| DOI: | 10.3109/10409239309082572 |
| Popis: | Proline residues confer unique structural constraints on peptide chains and markedly influence the susceptibility of proximal peptide bonds to protease activity. This review presents a critical analysis of peptidases involved in the cleavage of proline-containing peptide bonds, with particular attention to the role of proline peptidases in the regulation of the lifetime of biologically active peptides. Peptidases discussed include aminopeptidase P, prolidase, dipeptidyl peptidase IV, prolyl endopeptidase, and prolyl iminopeptidase. Attention is also given to HIV-1 protease, because this key enzyme processes an Xaa-Pro peptide bond. Analysis of the above enzymes reveals that they may function as key pacemakers in the control of the activity of many peptide hormones and that they are involved in a variety of immunological processes, including T-cell-mediated immune response. The novel occurrence of cis-trans isomerization about Xaa-Pro bonds and the biological function of peptidyl-prolyl cis-trans isomerases (immunophilins) are reviewed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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