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Zinc Carboxypeptidase
The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). Members of the H family have longer C-termini than those of family A, and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble. The zinc ligands have been determined as two histidines and a glutamate, and the catalytic residue has been identified as a C-terminal glutamate, but these do not form the characteristic metalloprotease HEXXH motif. Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by maki ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carboxypeptidase H
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 distribu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CPM (gene)
Carboxypeptidase M is an enzyme that in humans is encoded by the ''CPM'' gene. Function The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants Alternative splicing, or alternative RNA splicing, or differential splicing, is an alternative splicing process during gene expression that allows a single gene to code for multiple proteins. In this process, particular exons of a gene may be ... encoding the same protein have been described for this gene. References External links * Further reading * * * * * * * * * * * * * * * * * {{gene-12-stub ... [...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] |
CPD (gene)
Carboxypeptidase D is an enzyme that in humans is encoded by the ''CPD'' gene. Function The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities: the pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus binding protein. Transcript variants utilizing alternative polyadenylation Polyadenylation is the addition of a poly(A) tail to an RNA transcript, typically a messenger RNA (mRNA). The poly(A) tail consists of multiple adenosine monophosphates; in other words, it is a stretch of RNA that has only adenine bases. In euk ... signals exist for this gene. References Further reading * * * * * * * * * * External links * {{gene-17-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CPB2
Carboxypeptidase B2 (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable fibrinolysis inhibitor (TAFI), is an enzyme that, in humans, is encoded by the gene ''CPB2''. Function CPB2 is synthesized by the liverKaushansky K, Lichtman M, Beutler E, Kipps T, Prchal J, Seligsohn U. (2010; edition 8: pages 1833-1834 and 2040-2041) ''Williams Hematology''. McGraw-Hill. and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin/thrombomodulin complex, CPB2 exhibits carboxypeptidase activity. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen. Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as car ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CPA6
Carboxypeptidase A6 (CPA6) is a metallocarboxypeptidase enzyme that in humans is encoded by the ''CPA6'' gene. It is highly expressed in the adult mouse olfactory bulb and is broadly expressed in the embryonic brain and other tissues. The protein encoded by this gene belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino acid, and have functions ranging from digestion of food to selective biosynthesis of neuroendocrine peptides. Polymorphic variants and a reciprocal translocation t(6;8)(q26;q13) involving this gene, have been associated with Duane retraction syndrome. CPA6 processes several neuropeptides, including et and euenkephalin, angiotensin I, and neurotensin in vitro. Whereas CPA6 is capable of converting the enkephalins and neurotensin into inactive forms, it can convert the inactive angiotensin I into the active angiotensin II. CPA6 may have additional roles in processing peptides and proteins ''in vivo'', but the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CPA5
Carboxypeptidase A5 is an enzyme that in humans is encoded by the ''CPA5'' gene. Carboxypeptidases have functions ranging from digestion of food to selective biosynthesis Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. ... of neuroendocrine peptides. Members of the A/B subfamily of carboxypeptidases, such as CPA5, contain an approximately 90- amino acid pro region that assists in the folding of the active carboxypeptidase domain. Cleavage of the pro region activates the enzyme (Wei et al., 2002). upplied by OMIMref name="entrez" /> References External links * Further reading * * * * * * * {{refend ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CPA4 (gene)
Carboxypeptidase A4 is an enzyme that in humans is encoded by the ''CPA4'' gene. This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. This gene could be involved in the histone hyperacetylation pathway. It is imprinted and may be a strong candidate gene for prostate cancer Prostate cancer is cancer of the prostate. Prostate cancer is the second most common cancerous tumor worldwide and is the fifth leading cause of cancer-related mortality among men. The prostate is a gland in the male reproductive system that sur ... aggressiveness. References External links * * Further reading * * * * * * * {{gene-7-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CPA3
Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the ''CPA3'' gene. The "CPA3" gene expression has only been detected in mast cells and mast-cell-like lines, and CPA3 is located in secretory granules. CPA3 is one of 8-9 members of the A/B subfamily that includes the well-studied pancreatic enzymes carboxypeptidase A1 ( CPA1), carboxypeptidase A2 (CPA2), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. The enzyme now called CPA3 was originally named mast cell carboxypeptidase A, and another protein was initially called CPA3. A gene nomenclature committee renamed mast cell carboxypeptidase A as CPA3, and the original CPA3 reported by Huang et al. became CPA4 to reflect the order of their discovery. Structure Gene The "CPA3" gene is a 32kb-gene located at chromosome 3q24, consisting of 11 exons. Protein CPA3 shares significant homology with the CPA subfamily of metallopr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |