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Proprotein Convertase
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. History The phenomenon of prohormone conversion was discovered by Donald F. Steiner while examining the biosynthesis of insulin in 1967. At the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Furin
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 (FES Upstream Region) and therefore the protein was named furin. Furin is also known as PACE (Paired basic Amino acid Cleaving Enzyme). A member of family S8, furin is a subtilisin-like peptidase. Function The protein encoded by this gene is an enzyme that belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carboxypeptidase E
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. CPE is involved in the biosynthesis of most neuropeptides and peptide hormones. The production of neuropeptides and peptide hormones typically requires two sets of enzymes that cleave the peptide precursors, which are small proteins. First, proprotein convertases cut the precursor at specific sites to generate intermediates containing C-terminal basic residues (lysine and/or arginine). These intermediates are then cleaved by CPE to remove the basic residues. For some peptides, additional processing steps, such as C-terminal amidation, are subsequently required to generate the bioactive peptide, although for many peptides the action of the proprotein convertases and CPE is sufficient to produce the bioactive peptide. Tissue distribution ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PCSK5
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. Function The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein mediates posttranslational endoproteolytic processing for several integrin alpha subunits. It is thought to process prorenin, pro-membrane type-1 matrix metalloproteinase and HIV-1 glycoprotein gp160. Clinical significance Mutations in this gene have been associated with Currarino syndrome Currarino syndrome is an inherited congenital disorder where either the sacrum (the fused vertebrae forming the back of the pelvis) is not formed properly, or there is a mass in the p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PCSK4
Proprotein convertase subtilisin/kexin type 4 is an enzyme that in humans is encoded by the ''PCSK4'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a b .... References Further reading * * * * * * * * * * * {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PCSK3
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 (FES Upstream Region) and therefore the protein was named furin. Furin is also known as PACE (Paired basic Amino acid Cleaving Enzyme). A member of family S8, furin is a subtilisin-like peptidase. Function The protein encoded by this gene is an enzyme that belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proprotein Convertase 2
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 (and many other peptides), 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 activ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proprotein Convertase 1
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. Function PC1/3 is an enzyme that performs the proteolytic cleavage of prohormones to their intermediate (or sometimes completely cleaved) forms. It is present only in neuroendocrine cells such as brain, pituitary and adrenal, and most often cleaves after a pair of basic residues within prohormones but can occasionally cleave after a single arginine. It binds to a protein known as proSAAS, which also represents its endogenous inhibitor. PC1 is synthesized as a 99 kDa proform quickly converted to an 87 kDa major active form, which itself is nearly completely cleaved to a 66 kDa active form within neuroendocrine cells. Proprotein co ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Subtilisin
Subtilisin is a protease (a protein-digesting enzyme) initially obtained from '' Bacillus subtilis''. Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site. Subtilisins typically have molecular weights 27kDa. They can be obtained from certain types of soil bacteria, for example, '' Bacillus amyloliquefaciens'' from which they are secreted in large amounts. Nomenclature Subtilisin is also commercially known as ''Alcalase®'', ''Endocut-02L'', ''ALK-enzyme'', ''bacillopeptidase'', ''Bacillus subtilis alkaline proteinase bioprase'', ''bioprase AL'', ''colistinase'', ''genenase I'', ''Esperase®'', ''maxatase'', ''protease XXVII'', ''thermoase'', ''superase'', ''subtilisin DY'', ''subtilopeptidase'', ''SP 266'', ''Savinase®'', ''kazusase'', ''protease VIII'', ''protin A 3L'', ''Savinase®'', ''orientase 10B'', ''proteas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Wolfram Bode
Wolfram Bode (born March 8, 1942) is a German biochemist. Biography Born in Berlin, Bode was educated in chemistry and biochemistry at the University of Göttingen, the University of Tübingen and the University of Munich as a fellow of the Studienstiftung des deutschen Volkes. He obtained his Ph.D. in 1971 at the University of Munich for studies of the bacterial flagellum. Since 1972 he is working at the Max Planck Institute of Biochemistry in Martinsried. Bode is associate professor at the University of Munich. Career During his graduate studies Bode was using x-ray scattering. After his Ph.D. he then joined the lab of Robert Huber to work with x-ray crystallography. In 1975 Bode published the structure of trypsin, which was among the first protease structures that could be solved. His following work on the structure and function of proteins has contributed significantly to the understanding of several important biological processes, especially coagulation, fibrinolysis and p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Manual Than
{{disambiguation ...
Manual may refer to: Instructions * User guide * Owner's manual * Instruction manual (gaming) * Online help Other uses * Manual (music), a keyboard, as for an organ * Manual (band) * Manual transmission * Manual, a bicycle technique similar to a wheelie, but without the use of pedal torque * Manual, balancing on two wheels in freestyle skateboarding tricks * '' The Manual (How to Have a Number One the Easy Way)'' is a 1988 book by Bill Drummond and Jimmy Cauty See also * Instructions (other) * Tutorial A tutorial, in education, is a method of transferring knowledge and may be used as a part of a learning process. More interactive and specific than a book or a lecture, a tutorial seeks to teach by example and supply the information to complete ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gregory Petsko
Gregory A. Petsko (born August 7, 1948) is an American biochemist and member of the National Academy of Sciences, the National Academy of Medicine, the American Academy of Arts and Sciences, and the American Philosophical Society. He is currently Professor of Neurology at the Ann Romney Center for Neurologic Diseases at Harvard Medical School and Brigham and Women's Hospital. He formerly had an endowed professorship (the Arthur J. Mahon Chair) in Neurology and Neuroscience at Weill Cornell Medical College and is still an adjunct professor of Biomedical Engineering at Cornell University, and is also the Gyula and Katica Tauber Professor, Emeritus, in biochemistry and chemistry at Brandeis University. As of 2020 Petsko's research interests are understanding the biochemical bases of neurological diseases like Alzheimer's, Parkinson's, and ALS, discovering drugs (especially by using structure-based drug design) and biologics, especially gene therapy, that could therapeutically aff ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dagmar Ringe
Dagmar Ringe (born February 20, 1942) is an American biochemist, educator, and researcher. She is the Harold and Bernice Davis Professor in Aging and Neurodegenerative Disease at Brandeis University in Waltham, Massachusetts and holds appointments in the departments of Chemistry and Biochemistry. Education Ringe received the Bachelor's degree in Chemistry from Barnard College in New York, New York in 1963. She earned the doctoral degree in Chemistry under the direction of George Hein at Boston University in Boston, Massachusetts in 1969. Academic career Following postdoctoral research appointments at the Fakultat der Universitat Munchen in Munich, Germany and at the Massachusetts Institute of Technology (MIT) in Cambridge, Massachusetts, she became Instructor and Senior Lecturer in the Department of Chemistry at MIT. She joined the faculty at Brandeis University in 1990 as Lucille P. Markey Associate Professor, promoted to Lucille P. Markey Professor in 1994. She became the Haro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |