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In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.
Proprotein convertase 1, also known as prohormone convertase, prohormone convertase 3, or neuroendocrine convertase 1 and often abbreviated as PC1/3 is an enzyme that in humans is encoded by the PCSK1 gene. PCSK1 and PCSK2 differentially cleave proopiomelanocortin and they act together to process proinsulin and proglucagon in pancreatic islets.
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.
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.
Proprotein convertase 2 (PC2) also known as prohormone convertase 2 or neuroendocrine convertase 2 (NEC2) is a serine protease and proprotein convertase PC2, like proprotein convertase 1 (PC1), is an enzyme responsible for the first step in the maturation of many neuroendocrine peptides from their precursors, such as the conversion of proinsulin to insulin intermediates. To generate the bioactive form of insulin, a second step involving the removal of C-terminal basic residues is required; this step is mediated by carboxypeptidases E and/or D. PC2 plays only a minor role in the first step of insulin biosynthesis, but a greater role in the first step of glucagon biosynthesis compared to PC1. PC2 binds to the neuroendocrine protein named 7B2, and if this protein is not present, proPC2 cannot become enzymatically active. 7B2 accomplishes this by preventing the aggregation of proPC2 to inactivatable forms. The C-terminal domain of 7B2 also inhibits PC2 activity until it is cleaved into smaller inactive forms that lack carboxy-terminal basic residues. Thus, 7B2 is both an activator and an inhibitor of PC2. PC2 has been identified in a number of animals, including C. elegans.
Bone morphogenetic protein 1, also known as BMP1, is a protein which in humans is encoded by the BMP1 gene. There are seven isoforms of the protein created by alternate splicing.
Membrane-bound transcription factor site-1 protease, or site-1 protease (S1P) for short, also known as subtilisin/kexin-isozyme 1 (SKI-1), is an enzyme that in humans is encoded by the MBTPS1 gene. S1P cleaves the endoplasmic reticulum loop of sterol regulatory element-binding protein (SREBP) transcription factors.
Proprotein convertase subtilisin/kexin type 5 is an enzyme that in humans is encoded by the PCSK5 gene, found in chromosome 9q21.3 Two alternatively spliced transcripts are described for this gene but only one has its full length nature known.
Proprotein convertase subtilisin/kexin type 7 is an enzyme that in humans is encoded by the PCSK7 gene.
Proprotein convertase subtilisin/kexin type 6 is an protease that in humans is encoded by the PCSK6 gene which is located in chromosome 15. Pcsk6 is a calcium-dependent serine endoprotease that catalyzes the post-translational modification of precursor proteins from its ‘latent’ form to the cleaved ‘active’ form. Active Pcsk6 has been reported to process substrates such as transforming growth factor β, pro-albumin, von Willebrand factor, and corin. Clinically, Pcsk6 is suggested to play a role in left/right asymmetry, structural asymmetry of the brain, handedness, tumor progression, hemostasis, and cardiovascular diseases.
Proprotein convertase subtilisin/kexin type 4 is an enzyme that in humans is encoded by the PCSK4 gene.
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An Oligopeptidase is an enzyme that cleaves peptides but not proteins. This property is due to its structure: the active site of this enzyme is located at the end of a narrow cavity which can only be reached by peptides.
Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases includes is an enzyme. This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate, and catalyses the following chemical reaction
Cerevisin is an enzyme. This enzyme catalyses the following chemical reaction
Pestivirus NS3 polyprotein peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Magnolysin is an enzyme. This enzyme catalyses the following chemical reaction
Mitochondrial processing peptidase is an enzyme complex found in mitochondria which cleaves signal sequences from mitochondrial proteins. In humans this complex is composed of two subunits encoded by the genes PMPCA, and PMPCB. The enzyme is also known as. This enzyme catalyses the following chemical reaction
Proprotein convertase subtilisin/kexin type 1 inhibitor is a protein by the name of proSAAS that in humans is encoded by the PCSK1N gene.
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
- 1 2 3 "Kexin". Oxford Reference. Retrieved 2020-03-24.
- ↑ Seidah NG, Chrétien M (1994). Pro-protein convertases of subtilisin/kexin family. Methods in Enzymology. Vol. 244. Elsevier. pp. 175–88. doi:10.1016/0076-6879(94)44015-8. ISBN 978-0-12-182145-6. PMID 7845206.
- ↑ Rockwell NC, Krysan DJ, Komiyama T, Fuller RS (December 2002). "Precursor processing by kex2/furin proteases". Chemical Reviews. 102 (12): 4525–48. doi:10.1021/cr010168i. PMID 12475200.
- ↑ Julius D, Brake A, Blair L, Kunisawa R, Thorner J (July 1984). "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor". Cell. 37 (3): 1075–89. doi:10.1016/0092-8674(84)90442-2. PMID 6430565. S2CID 37772545.
- ↑ Achstetter T, Wolf DH (January 1985). "Hormone processing and membrane-bound proteinases in yeast". The EMBO Journal. 4 (1): 173–7. doi:10.1002/j.1460-2075.1985.tb02333.x. PMC 554167 . PMID 3894003.
- ↑ Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (October 1988). "Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases". Biochemical and Biophysical Research Communications. 156 (1): 246–54. doi:10.1016/s0006-291x(88)80832-5. PMID 2845974.
- ↑ Fuller RS, Brake A, Thorner J (March 1989). "Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease". Proceedings of the National Academy of Sciences of the United States of America. 86 (5): 1434–8. Bibcode:1989PNAS...86.1434F. doi: 10.1073/pnas.86.5.1434 . PMC 286710 . PMID 2646633.
- ↑ Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae". Biochemical and Biophysical Research Communications. 159 (1): 305–11. doi:10.1016/0006-291x(89)92438-8. PMID 2647083.
