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A lysosome is a membrane-bound organelle found in many animal cells. They are spherical vesicles that contain hydrolytic enzymes that can break down many kinds of biomolecules. A lysosome has a specific composition, of both its membrane proteins, and its lumenal proteins. The lumen's pH (~4.5–5.0) is optimal for the enzymes involved in hydrolysis, analogous to the activity of the stomach. Besides degradation of polymers, the lysosome is involved in various cell processes, including secretion, plasma membrane repair, apoptosis, cell signaling, and energy metabolism.
(2S,4R)-4-Hydroxyproline, or L-hydroxyproline (C5H9O3N), is an amino acid, abbreviated as Hyp or O, e.g., in Protein Data Bank.
A carboxypeptidase is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. At least two mechanisms have been discussed.
Carboxypeptidase E (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is encoded by the CPE gene. This enzyme catalyzes the release of C-terminal arginine or lysine residues from polypeptides.
Carboxypeptidase C is an enzyme. This enzyme catalyses the following chemical reaction
Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA gene.
The discovery of an orally inactive peptide from snake venom established the important role of angiotensin converting enzyme (ACE) inhibitors in regulating blood pressure. This led to the development of captopril, the first ACE inhibitor. When the adverse effects of captopril became apparent new derivates were designed. Then after the discovery of two active sites of ACE: N-domain and C-domain, the development of domain-specific ACE inhibitors began.
Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene.
Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.
Lysosomal Pro-X carboxypeptidase is an enzyme that in humans is encoded by the PRCP gene.
Xaa-Pro aminopeptidase 1 is an enzyme that in humans is encoded by the XPNPEP1 gene.
Carboxypeptidase A5 is an enzyme that in humans is encoded by the CPA5 gene.
Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Cathepsin X is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Lysine carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction:
Gly-Xaa carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Membrane Pro-Xaa carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
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References
- ↑ Walter R, Simmons WH, Yoshimoto T (April 1980). "Proline specific endo- and exopeptidases". Molecular and Cellular Biochemistry. 30 (2): 111–27. doi:10.1007/bf00227927. PMID 6991912.
- ↑ Odya CE, Erdös EG (1981). Human prolylcarboxypeptidase. Methods in Enzymology. Vol. 80 Pt C. pp. 460–6. doi:10.1016/s0076-6879(81)80040-7. PMID 7341916.
