Image Carboxypeptidase A.png thumb right 220px Carboxypeptidase A , from bovine pancreas A carboxypeptidase EC number 3.4.16 3.4.18 is a protease enzyme that Hydrolysis hydrolyzes cleaves the peptide bond of an amino acid Residue chemistry residue at the carboxy terminal C terminal end. Contrast with an aminopeptidase , which cleaves peptide bonds at the other end of the residue. Humans, animals, and plants ... requires a carboxypeptidase. Carboxypeptidases also function in blood clotting , growth ... carboxypeptidase or thiol carboxypeptidases EC number 3.4.18 . These names do not refer to the selectivity ... acids branched hydrocarbon chains are called carboxypeptidase A A for aromatic aliphatic . Carboxypeptidases that cleave positively charged amino acids arginine , lysine are called carboxypeptidase B B for Base chemistry basic . A metallo carboxypeptidase that cleaves a C terminal glutamate from the peptide N acetyl L aspartyl L glutamate is called glutamate carboxypeptidase . A serine carboxypeptidase ..., Xaa is any amino acid on the C terminus of a peptide is called prolyl carboxypeptidase . Activation ... form is referred to as a procarboxypeptidase . In the case of pancreatic carboxypeptidase A, the inactive zymogen form, pro carboxypeptidase A, is converted to its active form carboxypeptidase A by the enzyme enteropeptidase . This mechanism ensures that the cells wherein pro carboxypeptidase A is produced are not themselves digested. See also Carboxypeptidase E Carboxypeptidase A Enzyme category EC number 3.4 Thrombin activatable fibrinolysis inhibitor aka plasma carboxypeptidase B2 Transpeptidase bacterial transpeptidase , an alanine carboxypeptidase Bradykinin Metabolism bradykinin is broken down among other enzymes by carboxypeptidase N D Ala carboxypeptidase is a penicillin binding protein Phenylalanine might inhibit carboxypeptidase A External links MeshName Carboxypeptidases http ... Carboxypeptidase it Carbossipeptidasi he pl Karboksypeptydaza fi Karboksipeptidaasi ... more details
Image Carboxypeptidase A.png thumb right 220px Carboxypeptidase A, from bovine pancreas Carboxypeptidase A usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C terminal residues with aromatic or aliphatic side chain s. Most scientists in the field now refer to this enzyme as Gene CPA1 , and to a related pancreatic carboxypeptidase as Gene CPA2 . In addition, there are 4 other mammalian enzymes named CPA 3 through CPA 6, and none of these are expressed in the pancreas. Instead, these other CPA like enzymes have diverse functions. Gene CPA3 also known as mast cell CPA is involved in the digestion of proteins by mast cell s. Gene CPA4 previously known as CPA 3, but renumbered when mast cell CPA was designated CPA 3 may be involved in tumor progression, but this enzyme has not been well studied. Gene CPA5 and Gene CPA6 have also not been well studied. Interestingly, a human mutation of CPA 6 is known to cause Duane s syndrome abnormal eye movement . This, together with the localization of CPA 6 to embryonic eye muscle in addition to other limited locations suggests a role for CPA 6 in the control of neuronal migration axonal guidance. CPA 1 and CPA 2 and presumably all other CPAs contain a zinc atom at the active site. Loss of the zinc leads to loss of activity, which can be replaced easily by zinc, and also by some other divalent metals cobalt , nickel . See also CarboxypeptidaseCarboxypeptidase E External links The MEROPS online database for peptidases and their inhibitors http merops.sanger.ac.uk cgi bin merops.cgi?id M14.001 M14.001 MeshName Carboxypeptidases A Proteases Category Proteins Category Enzymes Category Metabolism id Karboksipeptidase A it Carbossipeptidasi A ... more details
protein Name carboxypeptidase B1 tissue caption image width HGNCid 2299 Symbol CPB1 AltSymbols EntrezGene 1360 OMIM 114852 RefSeq NM 001871 UniProt P15086 PDB ECnumber 3.4.17.2 Chromosome 3 Arm q Band 24 LocusSupplementaryData protein Name carboxypeptidase B2 carboxypeptidase B2 plasma caption image width HGNCid 2300 Symbol CPB2 AltSymbols EntrezGene 1361 OMIM 603101 RefSeq NM 016413 UniProt Q96IY4 PDB ECnumber Chromosome 13 Arm q Band 14.11 LocusSupplementaryData Carboxypeptidase B is a carboxypeptidase that preferentially acts upon basic amino acids, such as arginine and lysine. External links The MEROPS online database for peptidases and their inhibitors http merops.sanger.ac.uk cgi bin merops.cgi?id M14.003 M14.003 MeshName Carboxypeptidase B Proteases Category Proteins Category Enzymes Category Metabolism id Karboksipeptidase B ... more details
PBB geneid 1363 Carboxypeptidase E is an enzyme that in humans is encoded by the CPE gene . ref name ... Human carboxypeptidase E. Isolation and characterization of the cDNA, sequence conservation, expression ... pmid 2334405 pmc 1131319 doi ref ref name entrez cite web title Entrez Gene CPE carboxypeptidase E url ... to Stop updates. PBB Summary section title summary text Carboxypeptidase E cleaves C terminal amino ... secreted proteins. ref name entrez cite web title Entrez Gene CPE carboxypeptidase E url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1363 accessdate ref Carboxypeptidase E also called carboxypeptidase H, enkephalin convertase is found in neuroendocrine cells and in adrenal .... Carboxypeptidase E is found in all species of vertebrates that have been examined, and is also present in many other organisms that have been studied nematode, sea slug . Interestingly, carboxypeptidase E is not found in the fruit fly, and another enzyme presumably carboxypeptidase D fills in for carboxypeptidase E in this organism. Carboxypeptidase E appears to have several functions. The active form of carboxypeptidase E was shown to be in secretion secretory vesicle biology vesicles ... C terminal amino acids, producing the active form of the peptide. Products of carboxypeptidase E include ... associated carboxypeptidase E acts as a Protein targeting Targeting signals sorting signal for regulated ... for carboxypeptidase E remains controversial, and some evidence shows that this enzyme is not necessary for the sorting of regulated secretory proteins. Mice with mutant carboxypeptidase E, Cpe .... It is thought that a related enzyme carboxypeptidase D also contributes to neuropeptide processing and gives rise to the mature peptides in the Cpe sup fat sup mice. See also CarboxypeptidaseCarboxypeptidase ... enkephalin synthesizing carboxypeptidase localized to adrenal chromaffin granules. journal Proc. Natl ... in obese fat fat mice associated with a carboxypeptidase E mutation which reduces enzyme ... more details
Orphan date November 2010 Pfam box Symbol Peptidase M14 Name Zinc carboxypeptidase image width caption Pfam PF00246 InterPro IPR000834 SMART Prosite PDOC00123 SCOP 1cbx TCDB OPM family OPM protein PDB PDB3 1jqg A 127 412 PDB3 2c1c A 128 415 PDB3 1hee E 128 406 PDB3 2abz A 128 406 PDB3 1ell P 128 406 PDB3 1cps 128 406 PDB3 1bav D 128 406 PDB3 1m4l A 128 406 PDB3 1zlh A 128 406 PDB3 4cpa B 128 406 PDB3 1hdu D 128 406 PDB3 7cpa 128 406 PDB3 1cpx A 128 406 PDB3 1f57 A 128 406 PDB3 2ctb 128 406 PDB3 1arm 128 406 PDB3 5cpa 128 406 PDB3 3cpa A 128 406 PDB3 1ee3 P 128 406 PDB3 1yme 128 406 PDB3 1cbx 128 406 PDB3 1hdq A 128 406 PDB3 1pyt B 128 406 PDB3 8cpa 128 406 PDB3 6cpa 128 406 PDB3 1iy7 A 128 406 PDB3 2ctc 128 406 PDB3 1elm P 128 406 PDB3 1arl 128 406 PDB3 2boa B 129 408 PDB3 1aye A 127 404 PDB3 1dtd A 127 404 PDB3 1zg9 C 125 404 PDB3 1zg8 A 125 404 PDB3 1z5r A 125 404 PDB3 1nsa 125 404 PDB3 1zli A 125 404 PDB3 1kwm A 125 404 PDB3 1obr 113 402 PDB3 1uwy A 28 303 PDB3 1h8l A 16 291 The carboxypeptidase A family can be divided into two subfamilies carboxypeptidase H regulatory and carboxypeptidase A digestive ref name PUB00003579 cite journal author Rawlings ND, Barrett AJ title Evolutionary families of metallopeptidases journal Meth. Enzymol. volume 248 issue pages 183 228 year 1995 pmid 7674922 ref . Members of the H family have longer C termini than those of family A ref name PUB00003469 ..., Revina LP title Primary structure of carboxypeptidase T delineation of functionally relevant features in Zn carboxypeptidase family journal J. Protein Chem. volume 11 issue 5 pages 561 570 year 1992 pmid 1449602 ref , and carboxypeptidase M a member of the H family is bound to the membrane by a glycosylphosphatidylinositol ... WN, Rees DC, Lewis M title Refined crystal structure of carboxypeptidase A at 1.54 A resolution journal J. Mol. Biol. volume 168 issue 2 pages 367 387 year 1983 pmid 6887246 ref . Members of the carboxypeptidase ... AGBL4 AGBL5 AGTPBP1 CPA1 CPA2 CPA3 CPA4 CPA5 CPA6 CPB1 CPB2 CPD gene CPD Carboxypeptidase E CPE CPM ... more details
PBB geneid 1361 Carboxypeptidase B2 CPB2 also known as carboxypeptidase U CPU , plasma carboxypeptidase B pCPB , or thrombin activable fibrinolysis inhibitor TAFI is an enzyme that in humans is encoded by the CPB2 gene . ref name pmid1939207 cite journal author Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D title Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma journal J Biol Chem volume 266 issue 32 pages 21833 8 year 1991 month Dec pmid 1939207 pmc doi ref ref name pmid1427879 cite journal author Tsai SP, Drayna D title The gene encoding human plasma carboxypeptidase B CPB2 resides on chromosome 13 journal Genomics volume 14 issue 2 pages 549 50 year 1992 month Dec pmid 1427879 pmc doi 10.1016 S0888 7543 05 80268 X ref Function CPB2 ... carboxypeptidase activity. Activated CPB2 reduces fibrinolysis by removing the fibrin C terminus C ... 10.1021 bi990229v url issn ref Carboxypeptidase s 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 carboxypeptidase A cleaving aliphatic residues or carboxypeptidase B cleaving basic amino residues . The protein encoded by this gene is activated by thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis . ref name entrez cite web title Entrez Gene CPB2 carboxypeptidase ... isoforms. ref name entrez See also Carboxypeptidase B References reflist Further reading refbegin ... cite journal author Marinkovic DV, Marinkovic JN, Erd s EG, Robinson CJ title Purification of carboxypeptidase ... author Valnickova Z, Thogersen IB, Christensen S, et al. title Activated human plasma carboxypeptidase ... cite journal author Vanhoof G, Wauters J, Schatteman K, et al. title The gene for human carboxypeptidase ... Matsumoto A, Itoh K, Matsumoto R title A novel carboxypeptidase B that processes native beta amyloid ... more details
PBB geneid 1357 Carboxypeptidase A1 is an enzyme that in humans is encoded by the CPA1 gene . ref name entrez cite web title Entrez Gene CPA1 carboxypeptidase A1 pancreatic url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1357 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. Carboxypeptidase A1 is a monomeric pancreatic exopeptidase. It is involved in zymogen inhibition. ref name entrez cite web title Entrez Gene CPA1 carboxypeptidase A1 pancreatic url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1357 accessdate ref References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Catas s L, Villegas V, Pascual R, et al. title cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1. journal Biochem. J. volume 287 Pt 1 issue pages 299 303 year 1992 pmid 1417781 pmc 1133158 doi cite journal author Stewart EA, Craik CS, Hake L, Bowcock AM title Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31 qter. journal Am. J. Hum. Genet. volume 46 issue 4 pages 795 800 year 1990 pmid 1969228 pmc 1683655 doi cite journal author Moulard M, Michon T, Kerfelec B, Chapus C title Further studies on the human pancreatic binary complexes involving procarboxypeptidase A. journal FEBS Lett. volume 261 issue 1 pages 179 83 year 1990 pmid 2307232 doi 10.1016 0014 5793 90 80665 6 cite journal author Pascual R, Burgos FJ, Salva M, et al. title Purification and properties of five different forms of human procarboxypeptidases. journal Eur. J. Biochem. volume 179 issue 3 pages 609 16 year ... AY, Lalley PA, et al. title Assignment of the gene for carboxypeptidase A to human chromosome 7q22 ... more details
PBB geneid 1358 Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene . ref name pmid7896805 cite journal author Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M title The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three dimensional model journal J Biol Chem volume 270 issue 12 pages 6651 7 year 1995 month Apr pmid 7896805 pmc doi ref ref name pmid10860668 cite journal author Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T title Construction of a physical and transcript map flanking the imprinted MEST PEG1 region at 7q32 journal Genomics volume 66 issue 2 pages 221 5 year 2000 month Aug pmid 10860668 pmc doi 10.1006 geno.2000.6206 ref ref name entrez cite web title Entrez Gene CPA2 carboxypeptidase A2 pancreatic url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1358 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. The A2 form of pancreatic procarboxypeptidase acts on aromatic C terminal residues ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Pascual R, Burgos FJ, Salva M, et al. title Purification and properties of five different forms of human procarboxypeptidases. journal Eur. J. Biochem. volume 179 issue 3 pages 609 16 year 1989 pmid 2920728 doi 10.1111 j.1432 1033.1989.tb14590.x cite journal author Laethem RM, Blumenkopf TA, Cory M, et al. title Expression and characterization ... Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2. journal Nat. Struct. Biol. volume 7 issue 4 pages 322 8 year 2000 pmid ... more details
orphan date March 2010 Potato carboxypeptidase inhibitor PCI is a naturally occurring protease inhibitor peptide in potatoes that can form complexes with several Metalloexopeptidase metallo carboxypeptidase s, Enzyme inhibition inhibiting them in a strong competitive way with a Ki in the nanomolar range. ref 1 a br PCI consists of 39 amino acids molecular mass MW 4295 Atomic mass unit Da forming a 27 residue globular core stabilized by three disulfide bridge s and a C terminus C terminal tail with residues 35 39. PCI contains a small cysteine rich module, called a T knot scaffold , that is shared by several different protein families, including the Epidermal growth factor EGF family. ref 2,3,4 a Medicinal properties Because of the structural similarities with EGF, PCI inhibits tumor cell growth. ref 5 a Mechanism of action is inhibition of receptor dimerization and receptor phosphorylation trans autophosphorylation induced by epidermal growth factor EGF . PCI blocks the formation and activation of Epidermal growth factor receptor ErbB1 ErbB 2 EGFR and HER2 heterodimer s that have a prominent role in carcinoma development. ref 6 a br PCI also inhibits transforming growth factor alpha TGF alpha . In addition for pancreatic enzymes carboxypeptidase A and B, PCI also inhibits carboxypeptidase R without affecting the activity of carboxypeptidase N in the circulation and have therefore ... JM, Ryan CA title Carboxypeptidase inhibitor from potatoes journal Methods Enzymol. volume 80 issue ... C, Molina MA, Fern ndez Salas E, et al. title Potato carboxypeptidase inhibitor, a T knot protein, is an epidermal ... Aparicio C, et al. title Mechanism of action of potato carboxypeptidase inhibitor PCI as an EGF ..., Kuhn RW title Purification and properties of a carboxypeptidase inhibitor from potatoes journal J. Biol ... The disulfide folding pathway of potato carboxypeptidase inhibitor journal J. Biol. Chem. volume ... Protein kinase br Chemotherapy br Thrombolysis br Cancer research br DEFAULTSORT Potato Carboxypeptidase ... more details
enzyme Name glutamate carboxypeptidase II EC number 3.4.17.21 CAS number 111070 04 3 IUBMB EC number 3 4 17 21 GO code 0043275 image width caption PBB geneid 2346 Glutamate carboxypeptidase II GCPII also known as N acetyl L aspartyl L glutamate peptidase , NAAG peptidase , or NAALADase is an enzyme that in humans is encoded by the FOLH1 folate hydrolase prostate specific membrane antigen 1 gene . ref name pmid9838072 cite journal author O Keefe DS, Su SL, Bacich DJ, Horiguchi Y, Luo Y, Powell CT, Zandvliet D, Russell PJ, Molloy PL, Nowak NJ, Shows TB, Mullins C, Vonder Haar RA, Fair WR, Heston WD title Mapping, genomic organization and promoter analysis of the human prostate specific membrane antigen gene journal Biochim. Biophys. Acta volume 1443 issue 1 2 pages 113 27 year 1998 month November pmid 9838072 doi url issn ref Human GCPII contains 750 amino acids and weighs approximately 84 kD. ref name Barinka 2004 GCPII is a zinc Metalloprotein Metalloenzymes metalloenzyme that resides in membranes. Most of the enzyme resides in the extracellular space. GCPII is a class II membrane glycoprotein ... of glutamate carboxypeptidase II using a microplate assay journal Anal. Biochem. volume 310 ... BS, Konvalinka J, Hilgenfeld R title Structure of glutamate carboxypeptidase II, a drug target ... of which refer to the same protein glutamate carboxypeptidase II. Discovery GCPII is expressed in many ... K, Slusher BS, Konvalinka J title Identification of the N glycosylation sites on glutamate carboxypeptidase ... lacking glutamate carboxypeptidase II are protected from peripheral neuropathy and ischemic brain ... of glutamate carboxypeptidase II in human brain journal Neuroscience volume 144 issue 4 pages ... SM, Coyle JT, Herman MM, Hyde TM, Kleinman JE title Glutamate carboxypeptidase II gene expression ... simple, yet potent urea based inhibitors of glutamate carboxypeptidase II NAALADase journal ... Protein Data Bank http www.rcsb.org pdb home home.do Protein Data Bank MeshName Glutamate carboxypeptidase ... more details
Summary Information Description Carboxypeptidase A enzyme main chain trace. Gold plated brass model owned by William N. Lipscomb Jr. Model is of the mainchain. Each bend marks the position of an amino acid with about 13 atoms. Source I James S. Lipscomb created this work entirely by myself. Date Oct. 18, 2009 Author James S. Lipscomb photographer. Model built by Kathleen Seyfarth. other versions Category Molecules Category Proteins Category Enzymes Licensing self cc by sa 3.0 GFDL migration redundant ... more details
A metalloexopeptidase is a type of enzyme which acts as a metalloproteinase exopeptidase . The term metallocarboxypeptidase is sometimes used to describe a metalloexopeptidase carboxypeptidase . External links MeshName Metalloexopeptidase Proteases enzyme stub Category Enzymes Category EC 3.4.17 pt Metaloexopeptidase ... more details
Orphan date February 2009 PBB geneid 1359 Carboxypeptidase A3 mast cell carboxypeptidase A , also known as CPA3 , is an enzyme which in humans is encoded by the CPA3 gene . ref name entrez cite web title Entrez Gene CPA3 carboxypeptidase A3 mast cell url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1359 accessdate ref ref name pmid1729276 cite journal author Reynolds DS, Gurley DS, Austen KF title Cloning and characterization of the novel gene for mast cell carboxypeptidase A journal J. Clin. Invest. volume 89 issue 1 pages 273 82 year 1992 month January pmid 1729276 pmc 442845 doi 10.1172 JCI115571 url issn ref Function Altogether, there are 22 23 members of the metalloexopeptidase ... of the A B subfamily that includes the well studied pancreatic enzymes carboxypeptidase A1 carboxypeptidase A1 CPA1 , carboxypeptidase A2 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 Huang et al, 1999 . ref name Huang 1999 cite journal author Huang H, Reed CP, Zhang JS, et al. title Carboxypeptidase ... pmid 10383164 doi ref A gene nomenclature committee renamed mast cell carboxypeptidase A as CPA3, and the original ... name entrez cite web title Entrez Gene CPA3 carboxypeptidase A3 mast cell url http www.ncbi.nlm.nih.gov ... skin mast cell carboxypeptidase functional characterization, cDNA cloning, and genealogy. journal ... of the novel gene for mast cell carboxypeptidase A. journal J. Clin. Invest. volume 89 issue 1 pages ... CE, Proud D, et al. title Detection and partial characterization of a human mast cell carboxypeptidase ... carboxypeptidase A, and comparison of the protein with mouse mast cell carboxypeptidase A and rat ... CE, Kealey JT, Wintroub BU title Human mast cell carboxypeptidase. Purification and characterization ... mast cell carboxypeptidase. journal World J. Gastroenterol. volume 10 issue 3 pages 342 7 year 2004 ... more details
A transpeptidase EC 3.4.16.4 is a bacterial enzyme that cross link s the peptidoglycan chains to form rigid cell wall s. This enzyme is also known by several other names including DD peptidase , DD transpeptidase , D alanyl D alanine carboxypeptidase and serine type D Ala D Ala carboxypeptidase . ref cite web title E.C.3.4.16.4 Serine type D Ala D Ala carboxypeptidase work Enzyme Structures Database url http www.biochem.ucl.ac.uk bsm enzymes ec3 ec04 ec16 ec0004 index.html accessdate February 26, 2006 ref In gram positive bacteria, the peptidoglycan molecules are cross linked by a pentapeptide bridge, whereas in gram negative bacteria, the peptidoglycan molecules are directly covalently bound to each other. The protein transpeptidase is also known as Novel penicillin binding protein, which is necessary for cell wall peptidoglycan formation, and is inhibited by penicillin. The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl enzyme intermediate. Because of the interaction between penicillin and transpeptidase, this enzyme is also known as penicillin binding protein . References references External links The MEROPS online database for peptidases and their inhibitors http merops.sanger.ac.uk cgi bin merops.cgi?id S11.001 S11.001 EC number 3.4.16.4 MeshName Serine Type D Ala D Ala Carboxypeptidase Proteases Category EC 3.4.16 Category Bacteria Category Microbiology Bacteria stub es Transpeptidasa it Transpeptidasi he nl DD transpeptidase ... more details
Orphan date February 2009 PBB geneid 1368 Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene . ref name pmid8586455 cite journal author Kas K, Schoenmakers EF, Van de Ven WJ title Physical map location of the human carboxypeptidase M gene CPM distal to D12S375 and proximal to D12S8 at chromosome 12q15 journal Genomics volume 30 issue 2 pages 403 5 year 1996 month Mar pmid 8586455 pmc doi ref ref name entrez cite web title Entrez Gene CPM carboxypeptidase M url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1368 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates ... lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation ... have been described for this gene. ref name entrez cite web title Entrez Gene CPM carboxypeptidase ... PA, Becker RP, et al. title Carboxypeptidase M in brain and peripheral nerves. journal J. Neurochem ... for human membrane bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N ... author Skidgel RA, Davis RM, Tan F title Human carboxypeptidase M. Purification and characterization of a membrane bound carboxypeptidase that cleaves peptide hormones. journal J. Biol. Chem. volume ... Extracellular conversion of epidermal growth factor EGF to des Arg53 EGF by carboxypeptidase M ... of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc dependent proteases ... author Rehli M, Krause SW, Kreutz M, Andreesen R title Carboxypeptidase M is identical to the MAX.1 ... journal author Nagae A, Abe M, Becker RP, et al. title High concentration of carboxypeptidase M in lungs ... RA, McGwire GB, Li XY title Membrane anchoring and release of carboxypeptidase M implications for extracellular ... author Yoshioka S, Fujiwara H, Yamada S, et al. title Membrane bound carboxypeptidase M is expressed ... journal author Li XY, Skidgel RA title Release of glycosylphosphatidylinositol anchored carboxypeptidase ... more details
Orphan date February 2009 PBB geneid 1369 Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene . ref name pmid9628828 cite journal author Riley DA, Tan F, Miletich DJ, Skidgel RA title Chromosomal localization of the genes for human carboxypeptidase D CPD and the active 50 kilodalton subunit of human carboxypeptidase N CPN1 journal Genomics volume 50 issue 1 pages 105 8 year 1999 month Apr pmid 9628828 pmc doi 10.1006 geno.1998.5295 ref ref name pmid2912725 cite journal author Gebhard W, Schube M, Eulitz M title cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N kininase 1 journal Eur J Biochem volume 178 issue 3 pages 603 7 year 1989 month Mar pmid 2912725 pmc doi 10.1111 j.1432 1033.1989.tb14488.x ref ref name entrez cite web title Entrez Gene CPN1 carboxypeptidase N, polypeptide 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 1369 accessdate ref The PBB Summary .... PBB Summary section title summary text Carboxypeptidase N is a plasma metallo protease that cleaves ... with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency. ref name ... journal author Matthews KW, Mueller Ortiz SL, Wetsel RA title Carboxypeptidase N a pleiotropic regulator ... terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase ... D, Vingron M, Vriend G, et al. title On the specificity of carboxypeptidase N, a comparative study. journal ... author Sato T, Miwa T, Akatsu H, et al. title Pro carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not. journal J. Immunol. volume 165 issue 2 pages 1053 8 ... of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. journal Microbiol ... RA title DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase ... La Luz Sierra M, et al. title Identification of carboxypeptidase N as an enzyme responsible for C terminal ... more details
CTSA may refer to Cathepsin A is an enzyme which is classified both as a cathepsin and a carboxypeptidase. The Catholic Theological Society of America is a professional association of theologians that was founded in 1946 to promote studies and research in theology within the Catholic tradition. The Channel Tunnel Safety Authority The Clinical and Translational Science Award program is administered by the National Center for Research Resources, part of the U.S. National Institutes of Health. disambiguation ... more details
CPZ may be Cable Protection Zone, a zone protecting submarine telecommunications cable s from damage by anchors or fishing gear Charles Paddock Zoo , a community zoo in California Chlorpromazine , an antipsychotic drug, also called Thorazine, Stemetil or Largactil Circuit Park Zandvoort , a motorsport track near the town of Zandvoort, in the Netherlands Continuous permafrost zone .cpz, file extension of music text files used by COMPOZ programme see List of file formats alphabetical CPZ gene , a gene coding for the enzyme carboxypeptidase Z Disambig tr CPZ ... more details
Merge to Glutamate carboxypeptidase II discuss Talk Glutamate carboxypeptidase II Merger proposal date March 2011 Prostate specific membrane antigen PSMA is a type 2 integral membrane glycoprotein found in prostate tissues and a few other tissues. It is a possible therapeutic target for prostate cancer . Although it is a marker for prostate cancer little is known about its function in the body. PSMA is expressed on tumor cells as a noncovalent homodimer. ref http www.pnas.org content 100 22 12590.full ref It is being used in a nuclear medicine scanning procedure as the cellular target with injected radioactive labeled anti PSMA antibodies as markers to Molecular imaging image benign and malignant prostate acinar glandular tissue, whether in the gland or as cancer metastases elsewhere in the body. ref http www.nature.com pcan journal v3 n1 abs 4500390a.html ref Numerous clinical trials of cancer therapy are targeted at PSMA. ref name Olsen2007 cite web url http www.bentham.org rrct openaccessarticles rrct2 3 0004RRCT.pdf title Clinical Trials of Cancer Therapies Targeting Prostate Specific Membrane Antigen. author Olsen et al. year 2007 ref References reflist See also Molecular imaging Optical imaging Glutamate carboxypeptidase II External links http www.medicalnewstoday.com articles 138480.php Role Of Prostate Specific Membrane Antigen And Pepsinogen C Tissue Expression As An Adjunctive Method To Prostate Cancer Diagnosis http clincancerres.aacrjournals.org cgi content abstract 3 1 81 Prostate specific membrane antigen expression in normal and malignant human tissues http www.ncbi.nlm.nih.gov pubmed 9508077 Prostate specific membrane antigen current and future utility. biochem stub Category Tumor markers ... more details
Orphan date February 2009 PBB geneid 8532 Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene . ref name pmid9099699 cite journal author Song L, Fricker LD title Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase journal J Biol Chem volume 272 issue 16 pages 10543 50 year 1997 month May pmid 9099699 pmc doi 10.1074 jbc.272.16.10543 ref ref name entrez cite web title Entrez Gene CPZ carboxypeptidase Z url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8532 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text This gene encodes a member of the metallocarboxypeptidase family. This enzyme displays carboxypeptidase activity towards substrates with basic C terminal residues. It is most active at neutral pH and is inhibited by active site directed inhibitors of metallocarboxypeptidases. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Reznik SE, Fricker LD title Carboxypeptidases from A to z implications in embryonic development and Wnt binding. journal Cell. Mol. Life Sci. volume 58 issue 12 13 pages 1790 804 year 2002 pmid 11766880 doi 10.1007 PL00000819 cite journal author Gerhard DS, Wagner L, Feingold EA, et al. title The status, quality, and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC . journal Genome Res. volume 14 issue 10B pages 2121 7 year 2004 pmid 15489334 doi 10.1101 gr.2596504 pmc 528928 cite journal author Ota T, Suzuki Y, Nishikawa T, et al. title Complete sequencing and characterization of 21,243 full length human cDNAs. journal Nat. Genet. volume 36 issue ... title Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured ... more details
Orphan date February 2009 PBB geneid 51200 Carboxypeptidase A4 is an enzyme that in humans is encoded by the CPA4 gene . ref name pmid10383164 cite journal author Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI title Carboxypeptidase A3 CPA3 a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells journal Cancer Res volume 59 issue 12 pages 2981 8 year 1999 month Jul pmid 10383164 pmc doi ref ref name pmid10860668 cite journal author Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T title Construction of a physical and transcript map flanking the imprinted MEST PEG1 region at 7q32 journal Genomics volume 66 issue 2 pages 221 5 year 2000 month Aug pmid 10860668 pmc doi 10.1006 geno.2000.6206 ref ref name entrez cite web title Entrez Gene CPA4 carboxypeptidase A4 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 51200 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text 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 aggressiveness. ref name entrez cite web title Entrez Gene CPA4 carboxypeptidase A4 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 51200 accessdate ref References reflist Further ... T, et al. title The novel imprinted carboxypeptidase A4 gene CPA4 in the 7q32 imprinting domain ... chromosome 7q32 extends to the carboxypeptidase A gene cluster an imprinted candidate for Silver ... more details
An exopeptidase is an enzyme produced in the pancreas that catalyst catalyses the removal of an amino acid from the end of a polypeptide chain. Exopeptidase cleaves the end of a polypeptide chain. Aminopeptidase , an enzyme in the brush border of the small intestine, will cleave a single amino acid from the aminoterminal. Carboxypeptidase , which is a digestive enzyme present in pancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide. See also The Proteolysis Map Endopeptidase Edman degradation Dansyl chloride Protease External links MeshName Exopeptidases hydrolase stub Proteases Category Enzymes Category EC 3.4 de Exopeptidasen el fa it Esopeptidasi nl Exopeptidase pl Egzopeptydazy ru zh ... more details
the atomic structures of carboxypeptidase A ref name Hartsuck1965CPA ref name Lipscomb1965CPA ref name ..., W. N., The Low Resolution Structure of Carboxypeptidase A, Acta Cryst. 21 , A160 1966 . ref ref ... FA, Bethge PH, Ludwig ML, Steitz TA, Muirhead H, Coppola JC. The structure of carboxypeptidase A. VII ... of Carboxypeptidase A. III. Molecular Structure at 6 A Resolution, J Mol. Biol. 19 , 423 ..., T. A., Muirhead, H., Coppola, J. C., Reeke, G. N. and Quiocho, F. A., Molecular Structure of Carboxypeptidase ..., H., Searl, J., Steitz, T. A. and Lipscomb, W. N., Molecular Structure of Carboxypeptidase ... ML, Hartsuck JA, Steitz TA, Muirhead H, Coppola JC, Reeke GN, Lipscomb WN. The Structure of Carboxypeptidase ... ML, Quiocho FA, Steitz TA, Lipscomb WN. The structure of carboxypeptidase A. VI. Some Results ... more details
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