Difference between revisions of "Part:BBa K4020009"
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==Usage and Biology== | ==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). | + | 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). It is synthetic DNA. |
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==References== | ==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 | *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 | *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 | ||
Latest revision as of 20:40, 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). It is synthetic DNA.
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