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Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides. Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. Release of the granules from the cell is stimulated by either a hormonal signal or a nerve impulse, and the granules spill into a duct leading into the duodenum.
Oxytocin is a peptide hormone and neuropeptide normally produced in the hypothalamus and released by the posterior pituitary. Present in animals since early stages of evolution, in humans it plays roles in behavior that include social bonding, reproduction, childbirth, and the period after childbirth. Oxytocin is released into the bloodstream as a hormone in response to sexual activity and during labour. It is also available in pharmaceutical form. In either form, oxytocin stimulates uterine contractions to speed up the process of childbirth. In its natural form, it also plays a role in maternal bonding and milk production. Production and secretion of oxytocin is controlled by a positive feedback mechanism, where its initial release stimulates production and release of further oxytocin. For example, when oxytocin is released during a contraction of the uterus at the start of childbirth, this stimulates production and release of more oxytocin and an increase in the intensity and frequency of contractions. This process compounds in intensity and frequency and continues until the triggering activity ceases. A similar process takes place during lactation and during sexual activity.
Neurophysin I is a carrier protein with a size of 10 KDa and contains 90 to 97 amino acids. It is a cleavage product of preprooxyphysin. It is a neurohypophysial hormone that is transported in vesicles with oxytocin, the other cleavage product, along axons, from magnocellular neurons of the hypothalamus to the posterior lobe of the pituitary. Although it is stored in neurosecretory granules with oxytocin and released with oxytocin, its biological action is unclear.
Enteropeptidase is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment.
Furin is a protease, a proteolytic enzyme that in humans and other animals is encoded by the FURIN gene. Some proteins are inactive when they are first synthesized, and must have sections removed in order to become active. Furin cleaves these sections and activates the proteins. It was named furin because it was in the upstream region of an oncogene known as FES. The gene was known as FUR and therefore the protein was named furin. Furin is also known as PACE. A member of family S8, furin is a subtilisin-like peptidase.
Neurophysins are carrier proteins which transport the hormones oxytocin and vasopressin to the posterior pituitary from the paraventricular and supraoptic nucleus of the hypothalamus, respectively. Inside the neurosecretory granules, the analogous neurophysin I and II form stabilizing complexes via covalent interactions. Stabilizing neurophysin-hormone complexes that are formed within neurosecretory granules located in the posterior pituitary gland aid in intra-axonal transport. During intra-axonal transport, the neurophysin's are believed to prevent the bound hormone from leaking into the cytoplasmic space and proteolytic digestion via enzymes. However, due to the low concentration of neurophysin in the blood, it is likely the protein-hormone complex dissociates, indicating the neurophysin does not aid in transporting the hormone through the circulatory system.
Plasma kallikrein is an enzyme. This enzyme catalyses the following chemical reaction
Proprotein convertases (PPCs) are a family of proteins that activate other proteins. Many proteins are inactive when they are first synthesized, because they contain chains of amino acids that block their activity. Proprotein convertases remove those chains and activate the protein. The prototypical proprotein convertase is furin. Proprotein convertases have medical significance, because they are involved in many important biological processes, such as cholesterol synthesis. Compounds called proprotein convertase inhibitors can block their action, and block the target proteins from becoming active. Many proprotein convertases, especially furin and PACE4, are involved in pathological processes such as viral infection, inflammation, hypercholesterolemia, and cancer, and have been postulated as therapeutic targets for some of these diseases.
Neurophysin II is a carrier protein with a size of 19,687.3 Da and is made up of a dimer of two virtually identical chains of amino acids. Neurophysin II is a cleavage product of the AVP gene. It is a neurohypophysial hormone that is transported in vesicles with vasopressin, the other cleavage product, along axons, from magnocellular neurons of the hypothalamus to the posterior lobe of the pituitary. Although it is stored in neurosecretory granules with vasopressin and released with vasopressin into the bloodstream, its biological action is unclear. Neurophysin II is also known as a stimulator of prolactin secretion.
Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene.
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.
Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli LAP, and the solanaceous-specific acidic LAP (LAP-A) in tomato.
Kexin is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast. It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. The human homolog is PCSK4. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases, all kexins are eukaryotes. The enzyme is encoded by the yeast gene KEX2, and usually referred to in the scientific community as Kex2p. It shares structural similarities with the bacterial protease subtilisin. The first mammalian homologue of this protein to be identified was furin. In the mammal, kexin-like peptidases function in creating and regulating many differing proproteins.
Proprotein convertase subtilisin/kexin type 7 is an enzyme that in humans is encoded by the PCSK7 gene.
Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Leumorphin, also known as dynorphin B1–29, is a naturally occurring endogenous opioid peptide. Derived as a proteolytic cleavage product of residues 226-254 of prodynorphin, leumorphin is a nonacosapeptide and has the sequence Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr-Arg-Ser-Gln-Glu-Asp-Pro-Asn-Ala-Tyr-Ser-Gly-Glu-Leu-Phe-Asp-Ala. It can be further reduced to dynorphin B and dynorphin B-14 by pitrilysin metallopeptidase 1, an enzyme of the endopeptidase family. Leumorphin behaves as a potent and selective κ-opioid receptor agonist, similarly to other endogenous opioid peptide derivatives of prodynorphin.
Aminopeptidase B is an enzyme. This enzyme catalyses the following chemical reaction
Nardilysin is an enzyme. This enzyme catalyses the following chemical reaction
Howard Sachs, was a biochemist who helped pioneer the study of neuroendocrinology. His discoveries concerning the production of the hormone vasopressin laid the foundation for the field of hormone biosynthesis.
The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
References
- ↑ Clamagirand C, Creminon C, Fahy C, Boussetta H, Cohen P (September 1987). "Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytocin/neurophysin peptides at the basic amino acid doublet". Biochemistry. 26 (19): 6018–23. doi:10.1021/bi00393a011. PMID 2825769.
- ↑ Créminon C, Rholam M, Boussetta H, Marrakchi N, Cohen P (May 1988). "Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme". Journal of Chromatography. 440: 439–48. doi:10.1016/s0021-9673(00)94547-3. PMID 3042797.
- ↑ Brakch N, Boussetta H, Rholam M, Cohen P (September 1989). "Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model". The Journal of Biological Chemistry. 264 (27): 15912–6. PMID 2674120.
- ↑ Plevrakis I, Clamagirand C, Créminon C, Brakch N, Rholam M, Cohen P (March 1989). "Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor". Biochemistry. 28 (6): 2705–10. doi:10.1021/bi00432a051. PMID 2659078.
- ↑ Guillou MD, Camier M, Clamagirand C (August 1994). "Evidence for the presence of pro-oxytocin/neurophysin-converting enzyme in the human ovary". The Journal of Endocrinology. 142 (2): 345–52. doi:10.1677/joe.0.1420345. PMID 7931007.
