Difference between revisions of "Part:BBa K4020009"
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| − | + | ==Usage and Biology== | |
| + | Prolyl peptidase is a large enzyme that belongs to a distinct class of serine peptidases. Prolyl peptidase functions in immune and inflammatory responses and nutrient digestion. Prolyl peptidase cleaves C-terminally of proline residues in peptides which are at least 30 amino acids long (Fülöp et al., 1998). Its optimal pH is 4-5 (Shan et al., 2005). In human, prolyl peptidase is believed to be responsible for the maturation and degradation of peptide hormones and neuropeptides (Shan et al., 2005). | ||
| + | ==References== | ||
| + | *Fülöp, V., Böcskei, Z., & Polgár, L. (1998). Prolyl Oligopeptidase: An Unusual β-Propeller Domain Regulates Proteolysis. Cell, 94(2), 161–170. https://doi.org/10.1016/S0092-8674(00)81416-6 | ||
| + | *Shan, L., Mathews, I. I., & Khosla, C. (2005). Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity. PNAS March, 8(10), 2021. www.pdb.org | ||
Revision as of 20:36, 18 October 2021
Usage and Biology
Prolyl peptidase is a large enzyme that belongs to a distinct class of serine peptidases. Prolyl peptidase functions in immune and inflammatory responses and nutrient digestion. Prolyl peptidase cleaves C-terminally of proline residues in peptides which are at least 30 amino acids long (Fülöp et al., 1998). Its optimal pH is 4-5 (Shan et al., 2005). In human, prolyl peptidase is believed to be responsible for the maturation and degradation of peptide hormones and neuropeptides (Shan et al., 2005).
References
- Fülöp, V., Böcskei, Z., & Polgár, L. (1998). Prolyl Oligopeptidase: An Unusual β-Propeller Domain Regulates Proteolysis. Cell, 94(2), 161–170. https://doi.org/10.1016/S0092-8674(00)81416-6
- Shan, L., Mathews, I. I., & Khosla, C. (2005). Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity. PNAS March, 8(10), 2021. www.pdb.org