A family of gram-positive, saprophytic bacteria occurring in soil and aquatic environments.
A genus of gram-positive bacteria in the family Thermoactinomycetaceae, that can cause FARMER'S LUNG.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC and EC
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A genus of gram-positive bacteria that forms a branched mycelium. It commonly occurs as a saprophytic form in soil and aquatic environments.
A carboxypeptidase that is specific for proteins that contain two ALANINE residues on their C-terminal. Enzymes in this class play an important role in bacterial CELL WALL biosynthesis.
A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.
A ZINC-containing exopeptidase primarily found in SECRETORY VESICLES of endocrine and neuroendocrine cells. It catalyzes the cleavage of C-terminal ARGININE or LYSINE residues from polypeptides and is active in processing precursors of PEPTIDE HORMONES and other bioactive peptides.
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC and EC
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidase activity on some substrates. (From Enzyme Nomenclature, 1992) EC
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An antineoplastic agent with alkylating properties. It also acts as a mutagen by damaging DNA and is used experimentally for that effect.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.
An enzyme that catalyzes the transfer of methyl groups from S-adenosylmethionine to free carboxyl groups of a protein molecule forming methyl esters. EC 2.1.1.-.
A method for determining points of contact between interacting proteins or binding sites of proteins to nucleic acids. Protein footprinting utilizes a protein cutting reagent or protease. Protein cleavage is inhibited where the proteins, or nucleic acids and protein, contact each other. After completion of the cutting reaction, the remaining peptide fragments are analyzed by electrophoresis.
Methods used for studying the interactions of antibodies with specific regions of protein antigens. Important applications of epitope mapping are found within the area of immunochemistry.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
Books containing photographs, prints, drawings, portraits, plates, diagrams, facsimiles, maps, tables, or other representations or systematic arrangement of data designed to elucidate or decorate its contents. (From The ALA Glossary of Library and Information Science, 1983, p114)
Activities performed to identify concepts and aspects of published information and research reports.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.
Antibodies produced by a single clone of cells.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Immunoglobulins produced in response to VIRAL ANTIGENS.
An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC
An enzyme of the transferase class that catalyzes the reaction RNA(n+1) and orthophosphate to yield RNA(n) and a nucleoside diphosphate, or the reverse reaction. ADP, IDP, GDP, UDP, and CDP can act as donors in the latter case. (From Dorland, 27th ed) EC
Exclusive legal rights or privileges applied to inventions, plants, etc.
A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-
A peptide that is a homopolymer of glutamic acid.
Derivatives of folic acid (pteroylglutamic acid). In gamma-glutamyl linkage they are found in many tissues. They are converted to folic acid by the action of pteroylpolyglutamate hydrolase or synthesized from folic acid by the action of folate polyglutamate synthetase. Synthetic pteroylpolyglutamic acids, which are in alpha-glutamyl linkage, are active in bacterial growth assays.
Compounds based on a 7-membered heterocyclic ring including an oxygen. They can be considered a medium ring ether. A natural source is the MONTANOA plant genus. Some dibenzo-dioxepins, called depsidones, are found in GARCINIA plants.
A cytochrome oxidase inhibitor which is a nitridizing agent and an inhibitor of terminal oxidation. (From Merck Index, 12th ed)
A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.

Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. (1/106)

Several recently discovered members of the carboxypeptidase E (CPE) gene family lack critical active site residues that are conserved in other family members. For example, three CPE-like proteins contain a Tyr in place of Glu300 (equivalent to Glu270 of carboxypeptidase A and B). To investigate the importance of this position, Glu300 of rat CPE was converted into Gln, Lys, or Tyr, and the proteins expressed in Sf9 cells using the baculovirus system. All three mutants were secreted from the cells, but the media showed no enzyme activity above background levels. Wild-type CPE and the Gln300 point mutant bound to a p-aminobenzoyl-Arg-Sepharose affinity resin, and this binding was competed by an active site-directed inhibitor, guanidinoethylmercaptosuccinic acid. The affinity purified mutant CPE protein showed no detectable enzyme activity (<0.004% of wild-type CPE) toward dansyl-Phe-Ala-Arg. Expression of the Gln300 and Lys300 mutant CPE proteins in the NIT3 mouse pancreatic beta-cell line showed that these mutants are routed into secretory vesicles and secreted via the regulated pathway. Taken together, these results indicate that Glu300 of CPE is essential for enzyme activity, but not required for substrate binding or for routing into the regulated secretory pathway.  (+info)

Biosynthesis and packaging of carboxypeptidase D into nascent secretory vesicles in pituitary cell lines. (2/106)

Metallocarboxypeptidase D (CPD) is a membrane-bound trans-Golgi network (TGN) protein. In AtT-20 cells, CPD is initially produced as a 170-kDa endoglycosidase H-sensitive glycoprotein. Within 30 min of chase, the CPD increases to 180 kDa and is resistant to endoglycosidase H as a result of carbohydrate maturation. CPD also undergoes an activation step required for binding to a substrate affinity resin. Blocking the protein exit from the endoplasmic reticulum inhibits the increase in molecular mass but not the step required for affinity column binding, suggesting that enzyme activation precedes carbohydrate maturation and that these reactions occur in distinct intracellular compartments. Only the higher molecular weight mature CPD enters nascent secretory vesicles, which bud from the TGN of permeabilized AtT-20 and GH3 cells. The budding efficiency of CPD into vesicles is 2-3-fold lower than that of endogenous proopiomelanocortin in AtT-20 cells or prolactin in GH3 cells. In contrast, the packaging of a truncated form of CPD, which lacks the cytoplasmic tail and transmembrane domain, was similar to that of proopiomelanocortin. Taken together, the results support the proposal that CPD functions in the TGN in the processing of proteins that transit the secretory pathway and that the C-terminal region plays a major role in TGN retention.  (+info)

Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing. (3/106)

Five novel peptides were identified in the brains of mice lacking active carboxypeptidase E, a neuropeptide-processing enzyme. These peptides are produced from a single precursor, termed proSAAS, which is present in human, mouse, and rat. ProSAAS mRNA is expressed primarily in brain and other neuroendocrine tissues (pituitary, adrenal, pancreas); within brain, the mRNA is broadly distributed among neurons. When expressed in AtT-20 cells, proSAAS is secreted via the regulated pathway and is also processed at paired-basic cleavage sites into smaller peptides. Overexpression of proSAAS in the AtT-20 cells substantially reduces the rate of processing of the endogenous prohormone proopiomelanocortin. Purified proSAAS inhibits prohormone convertase 1 activity with an IC(50) of 590 nM but does not inhibit prohormone convertase 2. Taken together, proSAAS may represent an endogenous inhibitor of prohormone convertase 1.  (+info)

Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. (4/106)

Membrane carboxypeptidase E (CPE) is a sorting receptor for targeting prohormones, such as pro-opiomelanocortin, to the regulated secretory pathway in endocrine cells. Its membrane association is necessary for it to bind a prohormone sorting signal at the trans-Golgi network (TGN) to facilitate targeting. In this study, we examined the lipid interaction of CPE in bovine pituitary secretory granule membranes, which are derived from the TGN. We show that CPE is associated with detergent-resistant lipid domains, or rafts, within secretory granule membranes. Lipid analysis revealed that these rafts are enriched in glycosphingolipids and cholesterol. Pulse-chase and subcellular fractionation experiments in AtT-20 cells show that the association of CPE with membrane rafts occurred only after it reached the Golgi. Cholesterol depletion resulted in dissociation of CPE from secretory granule membranes and decreased the binding of prohormones to membranes. In vivo cholesterol depletion using lovastatin resulted in the lack of sorting of CPE and its cargo to the regulated secretory pathway. We propose that the sorting receptor function of CPE necessitates its interaction with glycosphingolipid-cholesterol rafts at the TGN, thereby anchoring it in position to bind to its prohormone cargo.  (+info)

Oligomerization of pro-opiomelanocortin is independent of pH, calcium and the sorting signal for the regulated secretory pathway. (5/106)

Studies indicate that pro-opiomelanocortin (POMC) is sorted to the regulated secretory pathway by binding to a sorting receptor identified as membrane-bound carboxypeptidase E (CPE) [Cool et al. (1997) Cell 88, 73-83]. The efficiency of this sorting mechanism could be enhanced if POMC molecules were to self-associate to form oligomers, prior or subsequent to binding to CPE. Using cross-linking and gel filtration techniques, we demonstrated that POMC forms oligomers at both neutral and acidic pHs and calcium was not necessary. delta N-POMC, which lacks the N-terminal sorting signal for the regulated secretory pathway, also formed similar oligomers, indicating that the sorting and oligomerization domains are different.  (+info)

Impaired prohormone convertases in Cpe(fat)/Cpe(fat) mice. (6/106)

A spontaneous point mutation in the coding region of the carboxypeptidase E (CPE) gene results in a loss of CPE activity that correlates with the development of late onset obesity (Nagert, J. K., Fricker, L. D., Varlamov, O., Nishina, P. M., Rouille, Y., Steiner, D. F., Carroll, R. J., Paigen, B. J., and Leiter, E. H. (1995) Nat. Genet. 10, 135-142). Examination of the level of neuropeptides in these mice showed a decrease in mature bioactive peptides as a result of a decrease in both carboxypeptidase and prohormone convertase activities. A defect in CPE is not expected to affect endoproteolytic processing. In this report we have addressed the mechanism of this unexpected finding by directly examining the expression of the major precursor processing endoproteases, prohormone convertases PC1 and PC2 in Cpe(fat) mice. We found that the levels of PC1 and PC2 are differentially altered in a number of brain regions and in the pituitary. Since these enzymes have been implicated in the generation of neuroendocrine peptides (dynorphin A-17, beta-endorphin, and alpha- melanocyte-stimulating hormone) involved in the control of feeding behavior and body weight, we compared the levels of these peptides in Cpe(fat) and wild type animals. We found a marked increase in the level of dynorphin A-17, a decrease in the level of alpha-melanocyte-stimulating hormone, and an alteration in the level of C-terminally processed beta-endorphin. These results suggest that the impairment in the level of these and other peptides involved in body weight regulation is mainly due to an alteration in carboxypeptidase and prohormone convertase activities and that this may lead to the development of obesity in these animals.  (+info)

ProSAAS processing in mouse brain and pituitary. (7/106)

ProSAAS is a newly discovered protein with a neuroendocrine distribution generally similar to that of prohormone convertase 1 (PC1), a peptide-processing endopeptidase. Several proSAAS-derived peptides were previously identified in the brain and pituitary of the Cpe(fat)/Cpe(fat) mouse based on the accumulation of C-terminally extended peptides due to the absence of enzymatically active carboxypeptidase E, a peptide-processing exopeptidase. In the present study, antisera against different regions of proSAAS were used to develop radioimmunoassays and examine the processing profile of proSAAS in wild type and Cpe(fat)/Cpe(fat) mouse tissues following gel filtration and reverse phase high performance liquid chromatography. In wild type mouse brain and pituitary, the majority of proSAAS is processed into smaller peptides. These proSAAS-derived peptides elute from the reverse-phase column in the same positions as synthetic peptides that correspond to little SAAS, PEN, and big LEN. Mass spectrometry revealed the presence of peptides with the expected molecular masses of little SAAS and big LEN in the fractions containing immunoreactive peptides. The processing of proSAAS is slightly impaired in Cpe(fat)/Cpe(fat) mice, relative to wild-type mice, leading to the accumulation of partially processed peptides. One of these peptides, the C-terminally extended form of PEN, is known to inhibit PC1 activity and this could account for the reduction in enzymatically active PC1 seen in Cpe(fat)/Cpe(fat) mice. The observation that little SAAS and big LEN are the major forms of these peptides produced in mouse brain and pituitary raises the possibility that these peptides function as neurotransmitters or hormones.  (+info)

Cholesterol, a cell size-dependent signal that regulates glucose metabolism and gene expression in adipocytes. (8/106)

Enlarged fat cells exhibit modified metabolic capacities, which could be involved in the metabolic complications of obesity at the whole body level. We show here that sterol regulatory element-binding protein 2 (SREBP-2) and its target genes are induced in the adipose tissue of several models of rodent obesity, suggesting cholesterol imbalance in enlarged adipocytes. Within a particular fat pad, larger adipocytes have reduced membrane cholesterol concentrations compared with smaller fat cells, demonstrating that altered cholesterol distribution is characteristic of adipocyte hypertrophy per se. We show that treatment with methyl-beta-cyclodextrin, which mimics the membrane cholesterol reduction of hypertrophied adipocytes, induces insulin resistance. We also produced cholesterol depletion by mevastatin treatment, which activates SREBP-2 and its target genes. The analysis of 40 adipocyte genes showed that the response to cholesterol depletion implicated genes involved in cholesterol traffic (caveolin 2, scavenger receptor BI, and ATP binding cassette 1 genes) but also adipocyte-derived secretion products (tumor necrosis factor alpha, angiotensinogen, and interleukin-6) and proteins involved in energy metabolism (fatty acid synthase, GLUT 4, and UCP3). These data demonstrate that altering cholesterol balance profoundly modifies adipocyte metabolism in a way resembling that seen in hypertrophied fat cells from obese rodents or humans. This is the first evidence that intracellular cholesterol might serve as a link between fat cell size and adipocyte metabolic activity.  (+info)

TY - JOUR. T1 - Cloning and sequence analysis of cDNA for bovine carboxypeptidase E. AU - Fricker, Lloyd D.. AU - Evans, Chris J.. AU - Esch, Fred S.. AU - Herbert, Edward. PY - 1986/12/1. Y1 - 1986/12/1. N2 - Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules1. A similar enzyme is present in many brain regions1,2 and in purified secretory granules from rat pituitary3 and rat insulinoma4. Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form1, which differ slightly in relative molecular mass (Mr)5. Here, to investigate whether the CPE activities in the various tissues are produced from a single gene, purified CPE was partially sequenced and oligonucleotide probes were used to isolate a clone encoding CPE from a bovine pituitary complementary DNA library. This cDNA hybridizes to bovine pituitary poly(A)+ ...
50) was found to have a mutation that deleted nearly the entire CPE gene. This patient had intellectual disability (inability to read or write) and had abnormal glucose homeostasis, similar to mice lacking CPE activity. In obesity, high levels of circulating free fatty acids have been reported to cause a decrease in the amount of carboxypeptidase E protein in pancreatic beta-cells, leading to beta-cell dysfunction (hyperproinsulinemia) and increased beta-cell apoptosis (via an increase in ER-stress). However, because CPE is not a rate-limiting enzyme for the production of most neuropeptides and peptide hormones, it is not clear how relatively modest decreases in CPE activity can cause physiological effects. Carboxypeptidase Carboxypeptidase A GRCh38: Ensembl release 89: ENSG00000109472 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000037852 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Entrez Gene: CPE carboxypeptidase E. Fricker LD (1988). ...
TY - JOUR. T1 - Quantitation of neuropeptides in Cpefat/Cpefat mice using differential isotopic tags and mass spectrometry. AU - Che, Fa yun. AU - Fricker, Lloyd D.. PY - 2002/7/1. Y1 - 2002/7/1. N2 - Neuroendocrine peptides play important roles as intercellular messengers. We previously developed a technique to isolate and identify a large number of neuroendocrine peptides from Cpefat/Cpefat mice (Che, F.; et al. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 9971-6); these mice lack carboxypeptidase E activity and this defect causes an accumulation of neuropeptide intermediates that contain C-terminal Lys or Arg residues (Naggert, J. K.; et al. Nat. Genet. 1995, 10, 135-42). In the present study, we have developed a differential isotopic-labeling technique that can be used to quantitate changes in neuropeptide levels in Cpefat/Cpefat mouse tissues. Samples are treated with either the H6 or the D6 form of acetic anhydride, peptides that contain C-terminal basic amino acids are isolated by affinity ...
Carboxypeptidase E (CPE) is a prohormone/proneuropeptide handling enzyme and mice bearing CPE mutations display an obese and diabetic phenotype. The melanocortin and neuropeptide Y (NPY) systems in the hypothalamus are also implicated in bone tissue redecorating since MC4R KO and NPY KO mice possess elevated BMD. However reduced amount of α-MSH the principal ligand of MC4R by up to 94% AZD2014 and having less detectable NPY in the hypothalamus of CPE KO usually do not ACAD9 recapitulate the single-gene KO phenotypes. This research highlights the complicated physiological interplay between peptides involved with energy fat burning capacity and bone tissue formation and moreover suggests the chance that sufferers bearing CPE and CART mutations resulting in inactive types of these substances could be at an increased threat of developing osteoporosis. carboxypeptidase E (CPE) is normally a digesting enzyme thats highly portrayed in endocrine cells and peptidergic neurons (17 19 It features to ...
2-Guanidinoethylmercaptosuccinic Acid - CAS 77482-44-1 - Calbiochem CAS 77482-44-1 Potent inhibitor of a carboxypeptidase B-like processing enzyme referred to as enkephalin convertase (Ki = 8.8 nM). - Find MSDS or SDS, a COA, data sheets and more information.
DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
Pauls, D., et al. Drosophila carboxypeptidase D (SILVER) is a key enzyme in neuropeptide processing required to maintain locomotor activity levels and survival rate. 10.1111/ejn.14516. Neuropeptides are processed from larger preproproteins by a dedicated set of enzymes. The molecular and biochemical mechanisms underlying preproprotein processing and the functional importance of processing enzymes are well‐characterised in mammals, but little studied outside this group. In contrast to mammals, Drosophila melanogaster lacks a gene for carboxypeptidase E (CPE), a key enzyme for mammalian peptide processing. By combining peptidomics and neurogenetics, we addressed the role of carboxypeptidase D (dCPD) in global neuropeptide processing and selected peptide‐regulated behaviours in Drosophila. We found that a deficiency in dCPD results in C‐terminally extended peptides across the peptidome, suggesting that dCPD took over CPE function in the fruit fly. dCPD is widely expressed throughout the ...
This gene encodes a member of the M14 family of metallocarboxypeptidases. The encoded preproprotein is proteolytically processed to generate the mature peptidase. This peripheral membrane protein cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters, including insulin. This protein may also function independently of its peptidase activity, as a neurotrophic factor that promotes neuronal survival, and as a sorting receptor that binds to regulated secretory pathway proteins, including prohormones. Mutations in this gene are implicated in type 2 diabetes. [provided by RefSeq, Nov 2015 ...
CPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 457 amino acids and having a molecular mass of 51.4kDa.
If you have a standard renewable certificate or you have voluntarily opted in to the certificate renewal system, you must obtain CPE from an SBEC-approved provider to renew your certificate. Existing school district-provided in-service should count toward the CPE requirement, as may other activities such as college coursework, professional seminars, mentoring and self-directed study. TCTA is an SBEC-approved provider. Members can earn CPE hours through TCTAs free online seminars.. One semester credit hour earned at an accredited institution of higher education is equivalent to 15 CPE clock hours.. Other than hours needed to comply with required topics for CPE (see below), CPE activities must be related to the certificate(s) being renewed and focus on the standards required for issuance of the certificate(s), including:. ...
The NIT-2 cell line was derived from the pancreatic beta cells of Cpe(fat)/Cpe(fat) mice by crossing C57BLKS/J-Cpe(fat)/+ mice with NOD/Lt-Tg(RIPTag)1Lt mice. The NIT-2 cell line was cultured from adenomatous islets obtained from a 10 week old F2 male and was compared with the NIT-1 cell line (ATCC-CRL-2055) previously developed from mice with wild-type CPE.
Kexin (EC is a prohormone processing protease found in the budding yeast (S. cerevisiae). It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. 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. The enzyme is also known as yeast KEX2 protease, proteinase yscF, prohormone-processing endoprotease, paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, endoproteinase Kex2p, gene KEX2 dibasic proteinase, Kex 2p proteinase, Kex2 endopeptidase, Kex2 endoprotease, Kex2 endoproteinase, Kex2 protease, proteinase Kex2p, Kex2-like precursor protein processing endoprotease, prohormone-processing KEX2 proteinase, prohormone-processing proteinase, proprotein ...
Qian, Y.M., Varlamov, O. and Fricker, L.D. (1999). Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. J. Biol. Chem. 274: 11582-11586. PMID 10206965. ...
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You ever go to a big party, go to the bathroom, flush the toilet, and the water starts coming … up? This is the most frightening moment in the life of a human being. Youll do anything to stop this. Youll lose your mind and start talking to the toilet: No, please, dont do this to me. No, come on, you know this is not my responsibility! I didnt make this happen! - Jerry Seinfeld. Of course you caused it to happen, Jerry. You flushed the toilet, which filled the bowl with water. More water went into the bowl than went out, and so it overflowed. Call any reputable plumber and ask why a toilet overflows, and thats the answer youll get: more water going in than going out.. Heh-heh-heh … just kidding. A reputable plumber would explain that something has clogged up the system, then charge you a hefty hourly fee to fix the clog.. Back in my standup days, I opened a few times for a comedian I really liked named Tom Parks. He had a good bit about his toilet backing up into his bathtub. (I dont ...
These fat greedy little beasties had reduced energy expenditure, and massive stores of ectopic fat, I.E. massive stores of fat in other places other than adipose tissue, aswell as increased circulating free fatty acids ( compared to mutant ATGL -/- mice that were fed a low-fat diet ). This is certainly what most top doctors would call a lipotoxic environment, and these greedy fat mice should be intensely diabetic. Theres just one problem ...
Lets start with the basics of what leptin is and what it does. It is known as the satiety hormone and this might help give you an idea of what it does. This is a hormone that inhibits hunger to help regulate energy balance. Heres the thing about this type of hormone, it has an antagonist, or a hormone that does the exact opposite, that is to make us feel hungry. The body works in this way to maintain a balance. This hormone is called ghrelin, the hunger hormone.. The problem with diets is that people think of them as a short-term plan that they will abandon once the fitness goal is achieved. They do not really make any lasting changes to their lifestyles. The other issue is that whenever you apply certain stress to the body, the body will always respond to compensate for any loss. In other words, if you make your body hungry, it will react by finding mechanisms to keep the energy balance, therefore, making you hungrier.. When leptin was first found to make fat mice lose weight, it was ...
As often happens with nutrition research, results from fasting research have been borrowed and packaged into ill-informed fad diets. Pandas research formed the basis of one such product, branded as The 8-Hour Diet. The book, cowritten by an editor at Mens Health, which covered Pandas research when it came out in 2012, claimed (right on the cover) that dieters who restricted their food consumption to an eight-hour window every day could watch the pounds disappear without watching what you eat! This idea, says Panda-who was not involved in producing the book-was unsupported by his research as of 2012. We never claimed that we could make fat mice lean with the eight-hour diet, he says. In our first paper, we just prevented obesity from happening.. Nevertheless, Panda has gone on to show that there may be some substance to the weight-loss hype. In addition to his experiments in mice, Pandas team found that flies, too, experienced benefits from restricting their feeding windows to a ...
In yet another set of experiments, the researchers fed mice a high-fat diet and allowed them to fully develop metabolic syndrome and obesity. Then they gave them the IAP supplement for six weeks. In these animals, IAP reduced endotoxin levels, inflammation and glucose intolerance. If the fat mice had taken the supplement for a longer period of time, their condition may have reversed even more ...
If there is one thing I have learned about my Husband over the years, it is this: Dont mess with his sleep. He is one of those individuals that requires at least eight hours a night, where as I can go on five and be all right. I have a video of him when I was about eight months pregnant and I have snuck into our bedroom while he is still asleep and am attempting to get him to wake up. I am saying all manner of nice and tempting things to get him to get up; offers of hot food drenched in syrup, mountain biking, nothing works. You finally see the corner of the pillow that is covering his head lift up and a voice comes out of the darkness underneath. He says, NO, Its too EFFING COLD OUTSIDE, NOW TAKE YOUR LITTLE DOG AND LEAVE ME ALONE. I WANT TO SLEEP. And then I can be heard doing what during my pregnancy Jeremy referred to as the Fat mouse Gus from Cinderella chuckle ...
Photos, videos, physical attributes and credits & experience of Daniel Gemsa - Actor, Extra and Model based in London, United Kingdom
PROTEIN - Protein is not required for protein itself, rather for the amino acids which make up the protein. Amino acids are required to maintain muscle, skin, coat etc. as well as provide enzymes and hormones for the correct functioning of the body. Two of the best protein sources are Egg (considered the perfect protein) and Chicken. XP3020 uses only high quality Egg and Chicken Meal as its source of quality protein.. FAT - Fat is extremely important for the dog, as dogs preferentially use fat for their energy source ie. it is the first ingredient the body uses to supply the energy needs of the dog. XP3020 uses only high quality Chicken Fat.. VITAMINS - The main function of Vitamins is as a catalyst for the body enzyme systems. They also help to resist disease and infection. Most vitamins must be provided in the diet.. MINERALS - These are only required in small amounts and must also be supplied in the diet. XP3020 uses only the best quality vitamins and minerals in suffcient ...
Many women find they pack on the pounds more easily than men do as they get older, and a new study on mice may help explain why.. After menopause, the activity of a particular enzyme involved in fat production -called Aldh1a1 - increases, the researchers said.. The enzyme is found in mice as well as people. During the study, female mice that ate a high-fat diet had more Aldh1a1 activity and made and stored more visceral fat (fat around the abdomen) than did male mice who ate a high-fat diet.. By contrast, female mice remained lean on a high-fat diet if they had been genetically engineered to lack the enzyme.. The female hormone estrogen appears to suppress Aldh1a1 activity. This might mean that younger women, who have high levels of estrogen, are protected against the enzymes undesirable effects. But after menopause, levels of estrogen decrease, causing Aldh1a1 activity to increase and making females vulnerable to weight gain.. By targeting Aldh1a1, researchers may be able to develop an obesity ...
ALTERNATIVE FOOD MOLECULES The catabolism of glucose is the most common metabolic pathway in cells. But animals also consume fats and proteins. These may be used to harvest energy. Fats Fats are built from long chain fatty acids and glycerol. They form triglycerides. The ...
We have cloned the cDNA for human carboxypeptidase D (CPD), a new B-type metallocarboxypeptidase that is membrane bound and has an acidic pH optimum. The 5.8 kb of cDNA sequenced contains an open reading frame of 4131 bp encoding 1377 amino acid residues. The sequence is similar (75% identity) to duck gp180, a protein that was isolated, cloned and sequenced as a hepatitis B virus-binding protein but not characterized as a carboxypeptidase. Hydropathic analysis revealed a hydrophobic region at the N-terminus, representing the signal peptide, and one near the C-terminus that probably represents the transmembrane anchor. The most striking feature is the presence of three tandem carboxypeptidase homology domains that have sequence similarity to the regulatory B-type carboxypeptidase family, typified by carboxypeptidases M, E and N. Because of the three repeats, CPD is about three times larger (175-180 kDa) than other members of this family (approx. 50-62 kDa). Domain 2 is most closely related to ...
Treatment of cultured bovine adrenal chromaffin cells with the catecholamine transport blocker reserpine was previously shown to increase enkephalin levels several-fold. To explore the biochemical mechanism of this effect, we examined the effect of reserpine treatment on the activities of three different peptide precursor processing enzymes: carboxypeptidase E (CPE) and the prohormone convertases (PCs) PC1/3 and PC2. Reserpine treatment increased both CPE and PC activity in extracts of cultured chromaffin cells; total protein levels were unaltered for any enzyme. Further analysis showed that the increase in CPE activity was due to an elevated Vmax, with no change in the Km for substrate hydrolysis or the levels of CPE mRNA. Reserpine activation of endogenous processing enzymes was also observed in extracts prepared from PC12 cells stably expressing PC1/3 or PC2. In vitro experiments using purified enzymes showed that catecholamines inhibited CPE, PC1/3 and PC2, with dopamine quinone the most ...
TY - JOUR. T1 - Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells. T2 - Localization to the trans-Golgi network and recycling from the cell surface. AU - Varlamov, Oleg. AU - Fricker, Lloyd D.. PY - 1998. Y1 - 1998. N2 - Carboxypeptidase D (CPD) is a recently discovered membrane-bound metallocarboxypeptidase that has been proposed to be involved in the post-translational processing of peptides and proteins that transit the secretory pathway. In the present study, the intracellular distribution of CPD was examined in AtT-20 cells, a mouse anterior pituitary-derived corticotroph. Antisera to CPD stain the same intracellular structures as those labeled with furin and wheat germ agglutinin. This distribution is distinct from carboxypeptidase E, which is localized to the secretory vesicles in the cell processes. The perinuclear distribution of CPD is detected even when the AtT-20 cells are treated with brefeldin A for 1-30 minutes, suggesting that CPD is present in the ...
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Mice (Cpefat/Cpefatand wild-type littermates) were obtained from The Jackson Laboratory (Bar Harbor, ME) and killed at 9-10 weeks of age. Brain, pituitary, and other tissues were removed and frozen on dry ice until analysis. Before freezing, a portion of the cerebral cortex was removed and used for purification of CPE to confirm the genotyping; only wild-type animals contain CPE that binds to the substrate affinity resin (Fricker et al., 1996; Varlamov et al., 1996). Brains from 10-20Cpefat/Cpefatmice or wild-type littermates were pooled and homogenized in 10 ml of boiling 0.1 m acetic acid. The homogenate was boiled for 10 min and then centrifuged at 50,000 × gfor 30 min at 4°C. The supernatant was filtered through a Centriplus-10 membrane (Amicon, Beverly, MA), and the flow through was combined with sodium acetate to give a final pH of 5.0. The material was applied to a 0.5 ml column containing immobilized anhydrotrypsin (Panvera). The column was washed with 0.5% ...
Bouma HR, Dugbartey GJ, Boerema AS, Talaei F, Herwig A, Goris M, van Buiten A, Strijkstra AM , Carey HV, Henning RH, Kroese FG. (2013) Reduction of body temperature governs neutrophil retention in hibernating and nonhibernating animals by margination. J Leukoc Biol Jun 13 [Epub ahead of print]. Herwig A, de Vries EM, Bolborea M, Wilson D, Mercer JG, Ebling FJ, Morgan PJ, Barrett P (2013) Hypothalamic ventricular ependymal thyroid hormone deiodinases are an important element of circannual timing in the Siberian hamster (Phodopus sungorus). PLoS One ,doi: 10.1371/journal.pone.0062003. Helwig M, Herwig A, Barrett P, Mercer J, Klingenspor M. (2013) Photoperiod-dependent regulation of carboxypeptidase E affects selective processing of neuropeptides in the seasonal Siberian hamster (Phodopus sungorus). J Neuroendocrinol 25:190-197. ...
To investigate the transcriptional regulation of the ACLP gene in VSMCs, we cloned and analyzed its promoter first in vitro and then in vivo. The single-copy mouse ACLP gene is composed of many small, closely spaced exons (Figure 1). The exon structure of the discoidin domain of ACLP is generally conserved with other discoidin domains containing proteins such as coagulation factor VIII37 and the discoidin domain tyrosine kinase receptors.38 In addition, the carboxypeptidase-like domain of mouse ACLP is similar in structure to the rat carboxypeptidase E gene.39 It is possible that ACLP could have been generated during evolution through the process of exon shuffling.40. The ACLP promoter is regulated in RASMCs via a strong positive element (−156 to −122) (Figure 4), which is bound and transactivated by Sp1 and Sp3 transcription factors (Figures 5 through 7⇑⇑). Sp1 and Sp3 are ubiquitously expressed proteins that regulate numerous genes.41 It is difficult to explain the regulation of VSMC ...
Define carboxypeptidase. carboxypeptidase synonyms, carboxypeptidase pronunciation, carboxypeptidase translation, English dictionary definition of carboxypeptidase. n. Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the end that contains a free carboxyl group
Fat percent of total calories - 33.6. Anyone care to read those figures and then explain to me how its too much fat that sparked a rise in obesity? Were we fatter in 1977, when we ate more of the stuff? Amazing … these people can see the evidence right in front of their academic faces, then draw conclusions that have nothing to do with it. Heres an another example of explaining away results they dont like:. One longitudinal study found no association between dietary energy density and adiposity among children who were followed annually from age 2 to 18 years (Alexy, 2005). Participants in this cohort were classified by dietary pattern into clusters based on percent energy from fat, with dietary energy density lowest at 3.7 (0.4) in the low fat cluster; 4.0 (0.4) in the medium fat intake; and highest at 4.1 (0.4) in the high fat cluster. Mean BMI during the study period differed significantly, with the highest BMI in the low fat, low dietary energy density cluster, a result the investigators ...
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HYPERPROINSULINEMIA description, symptoms and related genes. Get the complete information in our medical search engine for phenotype-genotype relation
carboxypeptidase L: Cathepsin A (also named protective protein and carboxypeptidase L) stabilizes beta-galactosidase and activates neuraminidase by forming with them a high-molecular-weight lysosomal complex
Also called: Lipids, Monounsaturated fat, Polyunsaturated fat, Saturated fat Fat is a major source of energy and aids your body in absorbing vitami...
Recycling instructions and/or packaging information. Substances or products causing allergies or intolerances: Milk. You can support our work by donating to Open Food Facts and also by using the Lilo search engine.Thank you! The product is in the fats category, the points for saturated fat are replaced by the points for the saturated fat / fat ratio. Open Food Facts is made by a non-profit association, independent from the industry. Sweet Cream Butter, Salted. Amount Per Serving. Personalized health review for Great Value Whipped Butter, Salted: 70 calories, nutrition grade (D plus), problematic ingredients, and more. 4%. tbsp. Code of conduct Instagram, This product page is not complete. Great Value. There are 100 calories in a 1 tbsp serving of Great Value Butter (Salted). Substances or products causing allergies or intolerances: → The analysis is based solely on the ingredients listed and does not take into account processing methods. SWEET CREAM SALTED BUTTER SAME GREAT TASTE Customers who ...
1 cm, respectively. The body mass index (BMI) was determined as weight/height2 (kg/m2). The biceps brachii, triceps brachii, subscapular, and suprailiac skinfold thicknesses were measured with a Harpenden caliper on the right side of the body with the subject in a standing position and are expressed as the mean of three Cilengitide manufacturer consecutive. measurements. The average of three measurements at each site was used to calculate the body density [16], percentage of body fat (%Fat), and lean body mass (LBM) [17]. All subjects were interviewed by experienced dietitians using a food frequency questionnaire Vactosertib chemical structure (FFQ), which is based on 29 food groups and 10 types of cooking, for estimating the energy and nutrient intakes of each subject during the past one to two months [18]. From FFQs, the selected mean daily dietary and nutrient intakes were calculated according to the Tables of Japanese Foodstuff Smoothened Agonist molecular weight Composition [19]. ...
CPXM1 - CPXM1 (untagged)-Human carboxypeptidase X (M14 family), member 1 (CPXM1), transcript variant 1 available for purchase from OriGene - Your Gene Company.
CPXM1 - CPXM1 (untagged)-Human carboxypeptidase X (M14 family), member 1 (CPXM1), transcript variant 1 available for purchase from OriGene - Your Gene Company.
Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
Lysosomal Pro-X Carboxypeptidase/PRCP Overexpression Lysate (Denatured). Tested Reactivity: Hu. Validated: WB. Backed by our 100% Guarantee.
1CBX: Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution.
Mouse Monoclonal Anti-Carboxypeptidase A1/CPA1 Antibody (1C12). Validated: WB, Flow, ICC/IF. Tested Reactivity: Human. 100% Guaranteed.
The present invention provides methods and compositions for the production of mature proteases in bacterial host cells. The compositions include modified polynucleotides that encode modified protease
thats a common mechanism in enzymes, not only in carboxypeptidase. However, the point is, there are several of these weak bonds and their sum is strong enough to stretch the peptide causing to be better to hydrolyse ...
In reply to Scott and colleagues,1 we found an unequivocally wide variation in reoperation after colorectal surgery. Furthermore, variation is identifiable at high surgical caseloads, suggesting that centralisation of surgical services, a policy commonly applied to reduce variation, may be ineffective. Our duty as researchers is to report variation when it clearly exceeds what would be expected by chance. The extent to … ...
Carboxypeptidases cleave at the carboxyl end of the protein. While they can catabolize proteins, they are more often used in ... "Carboxypeptidase". www.chemistry.wustl.edu. Retrieved 2019-03-23. Nelson DL, Cox MM, Lehninger AL (2013). Lehninger principles ... These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. ...
... some carboxypeptidase; low tyrosinase Aesthetics: pleasant fragrance; accumulation of flavoring compounds Color: low production ...
MPI Carboxypeptidase N deficiency; 212070; CPN1 Carcinoid tumors, intestinal; 114900; SDHD Cardiac arrhythmia, ankyrin-B- ...
... carboxypeptidase A2 (CPA2), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. ... Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the CPA3 ... and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases". Proceedings of the ... "Entrez Gene: CPA3 carboxypeptidase A3 (mast cell)". Reynolds DS, Gurley DS, Austen KF (January 1992). "Cloning and ...
Carboxypeptidase A5 is an enzyme that in humans is encoded by the CPA5 gene. Carboxypeptidases have functions ranging from ... "Entrez Gene: CPA5 carboxypeptidase A5". Human CPA5 genome location and CPA5 gene details page in the UCSC Genome Browser. ... Members of the A/B subfamily of carboxypeptidases, such as CPA5, contain an approximately 90-amino acid pro region that assists ... 2003). "The imprinted region on human chromosome 7q32 extends to the carboxypeptidase A gene cluster: an imprinted candidate ...
Carboxypeptidase A4 is an enzyme that in humans is encoded by the CPA4 gene. This gene is a member of the carboxypeptidase A/B ... "Entrez Gene: CPA4 carboxypeptidase A4". Human CPA3 genome location and CPA3 gene details page in the UCSC Genome Browser. Human ... Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI (Jul 1999). "Carboxypeptidase A3 (CPA3): a novel gene highly induced ... 2005). "Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the ...
... (EC, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is an enzyme. It ... Yaron A (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods in Enzymology. 45: 599-610. doi:10.1016/s0076-6879 ... Conlin CA, Miller CG (1995). "Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium ...
The structure of carboxypeptidase A. VI. Some Results at 2.0-A Resolution, and the Complex with Glycyl-Tyrosine at 2.8-A ... The Structure of Carboxypeptidase A, IV. Prelimitary Results at 2.8 A Resolution, and a Substrate Complex at 6 A Resolution. ... The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with ... "The Structure of Carboxypeptidase A. III. Molecular Structure at 6 A Resolution," J Mol. Biol. 19, 423-441 (1966). Ludwig, M. L ...
Retinoid-inducible serine carboxypeptidase is an enzyme that in humans is encoded by the SCPEP1 gene. GRCh38: Ensembl release ... Chen J, Streb JW, Maltby KM, Kitchen CM, Miano JM (Sep 2001). "Cloning of a novel retinoid-inducible serine carboxypeptidase ... "Entrez Gene: SCPEP1 serine carboxypeptidase 1". Robb GB, Rana TM (2007). "RNA helicase A interacts with RISC in human cells and ...
Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene. The "CPVL" gene is expressed ... "Entrez Gene: CPVL carboxypeptidase, vitellogenic-like". Harris J, Schwinn N, Mahoney JA, Lin HH, Shaw M, Howard CJ, da Silva RP ... Although the primary sequence of CPVL bears every hallmarks of a serine carboxypeptidase, the enzymatic function of CPVL has ... The designation of CPVL is a true serine carboxypeptidase. Although the primary sequence displays the expected serine ...
Carboxypeptidase A (left) was the first protein structure from Lipscomb's group. Carboxypeptidase A is a digestive enzyme, a ... Carboxypeptidase A digests by chopping off certain amino acids one-by-one from one end of a protein. The size of this structure ... "The Structure of Carboxypeptidase A, IV. Prelimitary Results at 2.8 A Resolution, and a Substrate Complex at 6 A Resolution". ... Carboxypeptidase A was a much larger molecule than anything solved previously. Aspartate carbamoyltransferase. (right) was the ...
1968 - Papain 1969 - Carboxypeptidase A is a zinc metalloprotease. Its crystal structure (PDB file 1CPA) showed the first ... Rees DC, Lipscomb WN (1982). "Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A ... Later a small protein inhibitor of carboxypeptidase was solved (PDB file 4CPA) that mechanically stops the catalysis by ... "The structure of carboxypeptidase A, VII. The 2.0-Å resolution studies of the enzyme and of its complex with glycyltyrosine, ...
... produces streptomycin II and carboxypeptidase. List of Streptomyces species LPSN bacterio.net ... "Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties". Biochemistry (Moscow). 75 (8): ...
"Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, ... Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene. The protein encoded by this gene is a membrane-bound ... "Entrez Gene: CPM carboxypeptidase M". Human CPM genome location and CPM gene details page in the UCSC Genome Browser. Fujiwara ... Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain ...
Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene. Carboxypeptidase N is a plasma ... 2000). "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not". J. Immunol. 165 (2 ... "Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.". Microbiol. Immunol. 46 (2): 131-4. doi ... "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1". Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets ...
Matthews KW, Mueller-Ortiz SL, Wetsel RA (Jan 2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Molecular ...
"Entrez Gene: CPN2 carboxypeptidase N, polypeptide 2". Human CPN2 genome location and CPN2 gene details page in the UCSC Genome ... Carboxypeptidase N subunit 2 is an enzyme that in humans is encoded by the CPN2 gene. GRCh38: Ensembl release 89: ... Riley DA, Tan F, Miletich DJ, Skidgel RA (Apr 1999). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) ... "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: ...
Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". ... carboxypeptidase A6 (CPA6), and angiotensin-converting enzyme (ACE). These enzymes are sometimes referred to as enkephalinases ... the resulting intermediates are further reduced by the enzyme carboxypeptidase E (CPE; previously known as enkephalin ...
Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". ... They include: Aminopeptidase N (APN) Neutral endopeptidase (NEP) Dipeptidyl peptidase 3 (DPP3) Carboxypeptidase A6 (CPA6) ...
The digestive enzyme carboxypeptidase became the second known zinc-containing enzyme in 1955. Zinc is the fourth most common ... Carboxypeptidase cleaves peptide linkages during digestion of proteins. A coordinate covalent bond is formed between the ... Two examples of zinc-containing enzymes are carbonic anhydrase and carboxypeptidase, which are vital to the processes of carbon ...
Probable carboxypeptidase X1 is an enzyme that in humans is encoded by the CPXM1 gene. The protein encoded by this gene is a ... "Entrez Gene: CPXM1 carboxypeptidase X (M14 family), member 1". Human CPXM1 genome location and CPXM1 gene details page in the ... member of the M14 family of zinc carboxypeptidases; however, the protein has no detectable carboxypeptidase activity. The ...
... the pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been ... "Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem ... Carboxypeptidase D is an enzyme that in humans is encoded by the CPD gene. The metallocarboxypeptidase family of enzymes is ... "Entrez Gene: CPD carboxypeptidase D". Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" ...
Carboxypeptidase, which is a protease that takes off the terminal amino acid group from a protein ...
There is evidence that the receptor in the closely related duck hepatitis B virus is carboxypeptidase D. The virions bind to ... Tong S, Li J, Wands JR (1999). "Carboxypeptidase D is an avian hepatitis B virus receptor". Journal of Virology. 73 (10): 8696- ...
CPN2: Carboxypeptidase N subunit 2. *CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental ...
... (EC, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... lysosomal carboxypeptidase B) is an enzyme. This enzyme catalyses the following chemical reaction Release of C-terminal amino ... A cysteine protease with unique carboxypeptidase activity". Biochemistry. 38 (39): 12648-54. doi:10.1021/bi991371z. PMID ...
It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin Z has an ... A cysteine protease with unique carboxypeptidase activity". Biochemistry. 38 (39): 12648-54. doi:10.1021/bi991371z. PMID ...
CS1 maint: discouraged parameter (link) Rees, DC; Lewis M (1983). "Refined crystal structure of carboxypeptidase a at 1.54 Å ...
... is a member of carboxypeptidase A protein family. The protein may function as a transcriptional repressor ... Muise AM, Ro HS (1999). "Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with ... Tumelty KE, Smith BD, Nugent MA, Layne MD (2014). "Aortic carboxypeptidase-like protein (ACLP) enhances lung myofibroblast ... Song L, Fricker LD (1997). "Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase". The Journal ...
Carboxypeptidase T (EC, CPT) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction ... an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases". Biochemistry ( ... Carboxypeptidase T at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281-288. doi:10.1111/j.1432- ...
D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. ... Zinc D-Ala-D-Ala carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Zinc D-Ala-D-Ala carboxypeptidase (EC, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, ... "The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". ...
Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, CPU, and thrombin- ... Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for ...
... an alanine carboxypeptidase bradykinin is broken down among other enzymes by carboxypeptidase N D-Ala carboxypeptidase is a ... The first carboxypeptidases studied were those involved in the digestion of food (pancreatic carboxypeptidases A1, A2, and B). ... Carboxypeptidase E Carboxypeptidase A Enzyme category EC number 3.4 Thrombin-activatable fibrinolysis inhibitor aka plasma ... In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active ...
Definition of carboxypeptidase A. Provided by Stedmans medical dictionary and Drugs.com. Includes medical terms and ... carboxypeptidase A. Pronunciation: kar-bok′sē-pep′ti-dās. Definition: A hydrolase that releases C-terminal amino acids, with ...
The term carboxypeptidase P may refer to: Lysosomal Pro-X carboxypeptidase Membrane Pro-X carboxypeptidase This set index page ...
Escherichia coli mutants defective in dipeptidyl carboxypeptidase. C E Deutch and R L Soffer ... Two independent mutants of Escherichia coli deficient in dipeptidyl carboxypeptidase activity (Dep-) were isolated after ... mutants may prove useful for delineating the regulation and cellular function of dipeptidyl carboxypeptidases in higher ... a potent inhibitor of mammalian dipeptidyl carboxypeptidase (angiotensin-converting enzyme, peptidyl dipeptidase, EC ...
carboxypeptidase synonyms, carboxypeptidase pronunciation, carboxypeptidase translation, English dictionary definition of ... carboxypeptidase. n. Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the ... Related to carboxypeptidase: dipeptidase, Carboxypeptidase B, Carboxypeptidase E, Carboxypeptidase c, carboxypeptidase G2 car· ... Carboxypeptidase - definition of carboxypeptidase by The Free Dictionary https://www.thefreedictionary.com/carboxypeptidase ...
This entry represents the carboxypeptidase domain found in carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and ... Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family.. J. ... The carboxypeptidase A family can be divided into four subfamilies: M14A (carboxypeptidase A or digestive), M14B ( ... Carboxypeptidase E in the mouse placenta.. Differentiation 74 648-60 2006. Rawlings ND, Barrett AJ. Evolutionary families of ...
Dipeptidyl carboxypeptidase definition at Dictionary.com, a free online dictionary with pronunciation, synonyms and translation ... Words nearby dipeptidyl carboxypeptidase. dip circle, DipCom, DipEd, dipeptidase, dipeptide, dipeptidyl carboxypeptidase, ...
Low P.S., Yuan J. (1996) Rapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting. In: Walker J.M. (eds) The ... Hayashi, R., Moore, S., and Stein, W. H. (1973) Carboxypeptidase from yeast:Large scale preparation and the application to COOH ...
Preferential cleavage:
Chowdhury C, Nayak TR, Young KD et al (2010) A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute ... Pal S., Ghosh A.S. (2019) PBP Isolation and DD-Carboxypeptidase Assay. In: Biswas I., Rather P. (eds) Acinetobacter baumannii. ... PBPs are also involved in PG remodeling by catalyzing DD-carboxypeptidase (DD-CPase) and endopeptidase reactions. Though the ... Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli. Trends ...
This article focuses on four human carboxypeptidases (CPs): two metallo-CPs and two serine CPs. The metallo-CPs are members of ... Cellular carboxypeptidases Immunol Rev. 1998 Feb;161:129-41. doi: 10.1111/j.1600-065x.1998.tb01577.x. ... This article focuses on four human carboxypeptidases (CPs): two metallo-CPs and two serine CPs. The metallo-CPs are members of ...
Similar to that of carboxypeptidase A EC, but with a preference for bulkier C-terminal residues. UniProt ...
Plasma carboxypeptidase B (CPB), which is activated by the thrombin/thrombomodulin complex, plays a procoagulant role during ...
Lysosomal protective protein, EC (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin ... CarboxypeptidaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, ... tr,U3KQU6,U3KQU6_HUMAN Carboxypeptidase OS=Homo sapiens OX=9606 GN=CTSA PE=1 SV=1 ...
Compare carboxypeptidase A4 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, ... carboxypeptidase A4 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool for ... Your search returned 53 carboxypeptidase A4 ELISA ELISA Kit across 8 suppliers. ...
Rabbit polyclonal Carboxypeptidase A antibody validated for WB and tested in Human, Mouse, Rat and Pig. Immunogen corresponding ... All lanes : Anti-Carboxypeptidase A antibody (ab63806) at 4 µg/ml. Lane 1 : Jurkat cell lysate. Lane 2 : Jurkat cell lysate. ... Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys ...
Compare carboxypeptidase, vitellogenic like ELISA Kits from leading suppliers on Biocompare. View specifications, prices, ... carboxypeptidase, vitellogenic like ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a widely used application for ... Your search returned 24 carboxypeptidase, vitellogenic like ELISA ELISA Kit across 3 suppliers. ...
Anti-Carboxypeptidase Y antibody conjugated to Biotin validated for WB, ELISA, IM, Dot. Immunogen corresponding to full length ... This antibody has been assayed against 1.0µg of Carboxypeptidase Y in a standard capture ELISA using Peroxidase conjugated ...
Human glutamate carboxypeptidase II (GCPII; EC is an established marker for prostate-cancer diagnosis as well as a ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II.. Barinka C1, Starkova J, Konvalinka J, ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst ...
Potent inhibitor of pancreatic carboxypeptidase A with a Ki of 27 nM, and of the serine proteases trypsin, chymotrypsin and ...
Downloading a figure as powerpoint requires a browser with javascript support. Enable javascript and try again For help please contact [email protected] ...
Carboxypeptidase Z an extracellular protein in zebrafish development. Historically the skeleton, in particular bone, was ... the protein carboxypeptidase Z (Cpz) was selected for further analysis. This peptidase has previously been implicated in the ...
Antibodies to human carboxypeptidase B and methods of use thereof. US5593674. Apr 27, 1995. Jan 14, 1997. Genentech, Inc.. ... Carboxypeptidases are proteases that hydrolyze the peptide bonds at the carboxy-terminal end of a chain of amino acids and have ... Plasma carboxypeptidase. US5837458. May 20, 1996. Nov 17, 1998. Maxygen, Inc.. Methods and compositions for cellular and ... Regulation of human zinc carboxypeptidase b-like protein. US20080003673 *. Sep 6, 2005. Jan 3, 2008. Alejandro Abuin. Novel ...
Browse our Carboxypeptidase M Lysate catalog backed by our Guarantee+. ... We offer Carboxypeptidase M Lysates for use in common research applications: Western Blot. Each Carboxypeptidase M Lysate is ... Our Carboxypeptidase M Lysates can be used in a variety of model species: Human. Use the list below to choose the ... Carboxypeptidase M lysate, CPM lysate, EC 3.4.17 lysate, EC lysate ...
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Cytosolic carboxypeptidase 4 (EC:3.4.17.-*Search proteins in UniProtKB for this EC number. ... sp,Q96MI9,CBPC4_HUMAN Cytosolic carboxypeptidase 4 OS=Homo sapiens OX=9606 GN=AGBL1 PE=1 SV=3 ...
Carboxypeptidase A1 Polyclonal Antibody from Invitrogen for Western Blot and Immunohistochemistry (Paraffin) applications. This ... Protein Aliases: Carboxypeptidase A1; carboxypeptidase A1 (pancreatic); CPA; pancreatic carboxypeptidase A Gene Aliases: CPA; ... Cite Carboxypeptidase A1 Polyclonal Antibody. The following antibody was used in this experiment: Carboxypeptidase A1 ... A synthetic peptide derived from the internal region of human CARBOXYPEPTIDASE A1 ...
  • Carboxypeptidase T ( EC , CPT ) is an enzyme . (wikipedia.org)
  • Zinc D-Ala-D-Ala carboxypeptidase (EC, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. (wikipedia.org)
  • 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 trypsin. (wikipedia.org)
  • Enzyme activity was highly sensitive to inhibition by 1-(D-3-mercapto-2-methylpropanoyl)-L-proline (SQ 14225), a potent inhibitor of mammalian dipeptidyl carboxypeptidase (angiotensin-converting enzyme, peptidyl dipeptidase, EC (pnas.org)
  • The "go or grow" poten-tial of gliomas is linked to the neuropeptide processing enzyme carboxypeptidase E and mediated by metabolic stress. (thefreedictionary.com)
  • With a New York University Cancer Institute colleague, the researchers reported that the mixture of free-floating blood proteins created by the enzyme carboxypeptidase N accurately predicted the presence of early-stage breast cancer tissue in mice and in a small population of human patients. (thefreedictionary.com)
  • Researchers from the Houston Methodist Research Institute and New York University Cancer Institute, conducted experiments on mice models and breast cancer patients, and found that a mixture of free-floating blood proteins created by carboxypeptidase N or CPN (an enzyme that plays a major role in modifying proteins after they are being created), accurately signalled the early stages of the deadly disease. (thefreedictionary.com)
  • PCR detection of the insertion/ deletion polymorphism of the human angiotensin converting enzyme gene (DCP1) (dipeptidyl carboxypeptidase 1). (thefreedictionary.com)
  • Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. (ebi.ac.uk)
  • Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity. (ebi.ac.uk)
  • The term carboxypeptidase P may refer to: Lysosomal Pro-X carboxypeptidase Membrane Pro-X carboxypeptidase This set index page lists enzyme articles associated with the same name. (wikipedia.org)
  • A high-resolution carboxypeptidase-Zn 2+ -citrate complex was studied by X-ray diffraction and enzyme kinetics for the first time. (hindawi.com)
  • The citrate molecule acts as a competitive inhibitor of this benchmark zinc-dependent peptidase, chelating the catalytic zinc ion in the active site of the enzyme and inducing a conformational change such that carboxypeptidase adopts the conformation expected to occur by substrate binding. (hindawi.com)
  • Production of MTX from MTX-Phe, catalyzed by bovine pancreas carboxypeptidase A (CPA), was 250-fold faster than the corresponding reaction involving methotrexate-α-alanine, previously the best MTX peptide substrate for the enzyme. (aacrjournals.org)
  • A carboxypeptidase B-like enzyme was detected in the soluble fraction of purified insulin secretory granules, and implicated in insulin biosynthesis. (portlandpress.com)
  • Human CPN (carboxypeptidase N) is a tetrameric plasma enzyme containing two glycosylated 83 kDa non-catalytic/regulatory subunits that carry and protect two active catalytic subunits. (biochemj.org)
  • Reduced expression of carboxypeptidase E (CPE), a neuropeptide-processing enzyme, in a cell death-resistant glioma cell line and lower CPE expression levels in the cohort of GBM samples of The Cancer Genome Atlas compared to normal brain control specimens prompted us to analyze the function of CPE as a putative tumor suppressor gene. (biomedsearch.com)
  • The D-alanyl-d-alanine carboxypeptidase enzyme is essential for virulence in the Schu S4 strain of Francisella tularensis and a dacD mutant is able to provide protection against a pneumonic challenge. (bioportfolio.com)
  • The enzyme L,D-carboxypeptidase A is involved in the recycling of bacterial peptidoglycan and is essential in Escherichia coli during stationary phase. (synbiosis.com)
  • Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. (creative-enzymes.com)
  • Glutamate carboxypeptidase II (GCPII) is an enzyme encoded by the FOLH1 (folate hydrolase 1) gene. (reportsnreports.com)
  • There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. (polstate.com)
  • Most scientists in the field now refer to this enzyme as CPA1 , and to a related pancreatic carboxypeptidase as CPA2 . (chemeurope.com)
  • The NH2-terminal amino acid sequence was determined and turned out to be identical to the NH2-terminal sequence of the membrane-bound carboxypeptidase M. By precipitation with antibodies MAX.1 and MAX.11, membrane preparations of macrophages and placental microvilli were almost completely depleted of enzyme activity, indicating that the two antibodies indeed recognize carboxypeptidase M. Immunoreactivity of both antibodies correlates with the reported tissue distribution of enzyme activity. (uni-regensburg.de)
  • Carboxypeptidase E is a peptide processing enzyme, involved in cleaving numerous peptide precursors, including neuropeptides and hormones involved in appetite control and glucose metabolism. (ox.ac.uk)
  • Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (wikipedia.org)
  • After the identification of potential regulatory proteins in the developing zebrafish skeleton during the MS-based approach, the protein carboxypeptidase Z (Cpz) was selected for further analysis. (wur.nl)
  • We offer Carboxypeptidase M Peptides and Carboxypeptidase M Proteins for use in common research applications: Blocking/Neutralizing, Control, ELISA, Protein Array, Western Blot. (novusbio.com)
  • Each Carboxypeptidase M Peptide and Carboxypeptidase M Protein is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • The protein encoded by CPA6 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. (antikoerper-online.de)
  • We show here that the Caenorhabditis elegans egl-21 gene encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the nervous system. (jneurosci.org)
  • Jager M, Lee MJ, Li C, Farmer SR, Fried SK, Layne MD. Aortic carboxypeptidase-like protein enhances adipose tissue stromal progenitor differentiation into myofibroblasts and is upregulated in fibrotic white adipose tissue. (harvard.edu)
  • The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. (genetex.com)
  • PGCP was co-purified from human placenta with lysosomal carboxypeptidase, cathepsin A, lysosomal endopeptidase, cathepsin D, and a gamma-interferon-inducible protein, IP-30, using an affinity chromatography on a Phe-Leu-agarose column. (sigmaaldrich.com)
  • Recombinant Rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids. (biovendor.com)
  • Analysis of the purified carboxypeptidase by SDS/polyacrylamide-gel electrophoresis under either reducing or non-reducing conditions showed it to be a monomeric protein of apparent Mr 55,000. (portlandpress.com)
  • In this study, the regulation of aortic carboxypeptidase-like protein (ACLP) expression in VSMCs was investigated. (ahajournals.org)
  • Carboxypeptidase B (EC, also well known as protaminase, pancreatic procarboxy-peptidase B (PCPB), tissue carboxypeptidase B, peptidyl-L-lysine (L-arginine) hydrolaseis a highly pancreas-specific protein (PASP), and has been identified previously as a serum marker for acute pancreatitis and pancreatic graft rejection. (creative-enzymes.com)
  • Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. (creativebiomart.net)
  • Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC - Glutamate carboxypeptidase II (GCPII) is a membrane-bound binuclear zinc metallopeptidase with the highly expressed in nervous and prostatic tissue. (reportsnreports.com)
  • Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC pipeline Target constitutes close to 9 molecules. (reportsnreports.com)
  • The latest report Glutamate Carboxypeptidase 2 - Pipeline Review, H2 2017, outlays comprehensive information on the Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type. (reportsnreports.com)
  • It also reviews key players involved in Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC targeted therapeutics development with respective active and dormant or discontinued projects. (reportsnreports.com)
  • Recombinant trypsin,recombinant carboxypeptidase B and recombinant protein A won the Shanghai high-tech achievement transformation project in Sep.2013. (polstate.com)
  • Additionally, the report provides an overview of key players involved in Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC targeted therapeutics development and features dormant and discontinued projects. (globalmarketsdirect.com)
  • The report analyses the pipeline products from therapy areas Oncology, Central Nervous System and Toxicologyunder development targeting Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC (globalmarketsdirect.com)
  • Our laboratory has identified a secreted matrix protein, aortic carboxypeptidase-like protein (ACLP), which is upregulated in idiopathic pulmonary fibrosis. (bu.edu)
  • Recommended name: Cytosolic carboxypeptidase-like protein 5 EC= 3.4.17. (cusabio.com)
  • It contains Human Carboxypeptidase A2 capture antibody, Human Carboxypeptidase A2 detector antibody (HRP) and a highly purified HEK293-expressed recombinant Human Carboxypeptidase A2 protein. (sinobiological.com)
  • Prostate-Specific Membrane Antigen (PSMA) is a transmembrane glutamate carboxypeptidase expressed on tumor-associated vasculature that positively regulates angiogenesis in a laminin-dependent manner. (thefreedictionary.com)
  • Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. (thefreedictionary.com)
  • A high-resolution structure of ligand-free human glutamate carboxypeptidase II. (nih.gov)
  • 11CMCG: Synthesis, uptake selectivity, and primate PET of a probe for glutamate carboxypeptidase II (NAALADase). (thefreedictionary.com)
  • Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate carboxypeptidase/prostate-specific membrane antigen. (sigmaaldrich.com)
  • We describe the identification, cDNA cloning, and biochemical characterization of a new human blood plasma glutamate carboxypeptidase (PGCP). (sigmaaldrich.com)
  • PGCP showed significant amino acid sequence homology to several cocatalytic metallopeptidases including a glutamate carboxypeptidase II also known as N-acetyl-aspartyl-alpha-glutamate carboxypeptidase or as prostate-specific membrane antigen and expressed glutamate carboxypeptidase activity. (sigmaaldrich.com)
  • ZJ 43 is a potent inhibitor of PSM and PSMAL (glutamate carboxypeptidase II and III). (adooq.com)
  • 2-MPPA is a selective glutamate carboxypeptidase II (GCP-II) inhibitor used in the treatment of neurological disorders associated with excessive activation of glutamatergic systems. (adooq.com)
  • Inhibition of glutamate carboxypeptidase II (GCPII) has been shown to be neuroprotective in multiple preclinical models in which dysregulated glutamatergic transmission is implicated. (elsevier.com)
  • A series of hydroxamic acids has been prepared as potential inhibitors of glutamate carboxypeptidase II (GCP II). (elsevier.com)
  • Here we report a novel mechanism by which secreted plasma glutamate carboxypeptidase(PGCP) negatively involves Wnt/β-catenin signaling by DKK4 regulation in liver cancer metastasis. (oncotarget.com)
  • Glutamate carboxypeptidase II (GCPII) is a membrane-bound binuclear zinc metallopeptidase with the highest expression levels found in the nervous and prostatic tissue. (eurekaselect.com)
  • C. Barinka, C. Rojas, B. Slusher and M. Pomper, " Glutamate Carboxypeptidase II in Diagnosis and Treatment of Neurologic Disorders and Prostate Cancer", Current Medicinal Chemistry (2012) 19: 856. (eurekaselect.com)
  • Enzymes that use a metal in the active site are called "metallo-carboxypeptidases" (EC number 3.4.17). (wikipedia.org)
  • 14) Furthermore, environmental exposures, concomitant medication regimens, and the activities of other metabolic enzymes (eg, ACE, carboxypeptidase N) are also likely to influence bradykinin degradation and the risk for acute hypotensive transfusion reactions. (thefreedictionary.com)
  • Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. (thermofisher.com)
  • According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). (thermofisher.com)
  • The Arabidopsis ( Arabidopsis thaliana ) genome encodes 51 proteins annotated as serine carboxypeptidase-like (SCPL) enzymes. (plantphysiol.org)
  • Deconjugation by pure carboxypeptidase A and B was also examined, and hydrolysis by these tissue fluids and enzymes was compared with that mediated by a bacterial cholyglycine hydrolase. (eurekamag.com)
  • Studies using pure enzymes showed that bovine carboxypeptidase A hydrolyzed the cholyl conjugates of the neutral L-.alpha. (eurekamag.com)
  • Shanghai Yaxin Biotechnology company was founded in 2008,which is a high-tech enterprise that focuses on researching and producing the recombinant proteins.YaxinBio is the first and only a company on researching and producing the recombinant carboxypeptidase B and recombinant trypsin.Animal original free enzymes are specially used in the human recombinant insulin production,and exporting abroad. (polstate.com)
  • 1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating proteases activities found in extracted enzymes with lower purity level. (polstate.com)
  • Carboxypeptidase B from Creative Enzymes has been used as a reference for assaying carboxypeptidase activity in lysed pituitary granules derived from the anterior and intermediate lobes of rat. (creative-enzymes.com)
  • This antibody has been assayed against 1.0µg of Carboxypeptidase Y in a standard capture ELISA using Peroxidase conjugated streptavidin and ABTS (2,2'-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) as a substrate for 30 minutes at RT. (abcam.com)
  • The following antibody was used in this experiment: Carboxypeptidase A1 Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-39610, RRID AB_2556162. (thermofisher.com)
  • Carboxypeptidase M Polyclonal antibody specifically detects Carboxypeptidase M in Human samples. (fishersci.com)
  • Carboxypeptidase B2/CPB2 Polyclonal antibody specifically detects Carboxypeptidase B2/CPB2 in Human samples. (fishersci.com)
  • Carboxypeptidase B antibody LS-C713312 is an HRP-conjugated rabbit polyclonal antibody to Carboxypeptidase B (CPB) from human, mouse and rat. (lsbio.com)
  • Carboxypeptidase B antibody LS-C503531 is an AP-conjugated rabbit polyclonal antibody to human Carboxypeptidase B (CPB). (lsbio.com)
  • Immunoperoxidase staining of human pancreas with Rabbit anti Bovine carboxypeptidase A1 antibody ( AHP2054 ) and HISTAR detection kit . (bio-rad-antibodies.com)
  • Rabbit anti Bovine Carboxypeptidase A1 antibody used for the evaluation of carboxypepridase and pro-carboxypeptidase in mouse tissue lysates by western blotting. (bio-rad-antibodies.com)
  • Antigens Carboxypeptidase A2_CPA2 antibody storage GENTAUR recommends for long therm storage to freeze at -24 C. For short time storage up to 30 days we suggest fridge storage at 1 to 10 C. Prevent multiple freeze taw cycles of Antigens Carboxypeptidase A2_CPA2. (antibody-antibodies.com)
  • Potent inhibitor of pancreatic carboxypeptidase A with a Ki of 27 nM, and of the serine proteases trypsin, chymotrypsin and pancreatic elastase, with Ki values of 6.9 nM, 1.83 nM and 4 nM, respectively. (rcsb.org)
  • 1998). Among the studied inhibitors, only two are specific for MCP, i.e. , the potato carboxypeptidase inhibitor (PCI) and its close homolog found in tomato plants (TCI). (bio-protocol.org)
  • Enhanced Co 2+ activation and inhibitor binding of carboxypeptidase M at low pH. (portlandpress.com)
  • Carboxypeptidase G2 (CPG2) Inhibitor is a novel Carboxypeptidase G2 (CPG2) Inhibitor, Antitumor agents. (adooq.com)
  • The inhibitor appeared to cause lysis of E. coli during stationary phase, behavior that is similar to a previously described deletion mutant of L,D-carboxypeptidase A (M. F. Templin, A. Ursinus, and J.-V. Holtje, EMBO J. 18:4108-4117, 1999). (synbiosis.com)
  • CPR (identical to carboxypeptidase U [CPU], plasma carboxypeptidase B [plasma CPB]) has also been described as an inhibitor of fibrinolysis, and termed TAFI (thrombin activatable fibrinolysis inhibitor). (biomedcentral.com)
  • Herein, we report the discovery of β-lybatide, a novel carboxypeptidase inhibitor belonging to a different CRP family from the wolfberry plant. (ntu.edu.sg)
  • Biochemical assays showed that β-lybatide is a potent carboxypeptidase inhibitor which could contribute to the wolfberry biological activities. (ntu.edu.sg)
  • Together, our results show that β-lybatide is the first and the smallest plant-derived hyperstable carboxypeptidase inhibitor discovered from a functional food. (ntu.edu.sg)
  • Expression of carboxypeptidase M on mRNA level and enzymatic activity markedly increase during in vitro differentiation of monocytes, according to the described increase in MAX.1 and MAX.11 antigen expression. (uni-regensburg.de)
  • Other carboxypeptidases that use active site serine residues are called "serine carboxypeptidases" (EC number 3.4.16). (wikipedia.org)
  • Similar to that of carboxypeptidase A EC , but with a preference for bulkier C-terminal residues. (rcsb.org)
  • carboxypeptidase A removes aromatic or branched hydrocarbons, while carboxypeptidase B removes positively charged terminal lysine or arginine amino acid residues. (thefreedictionary.com)
  • The presence of a codon for isoleucine at the residues corresponding to codon 255 of rat CPA1 cDNA strongly suggests that the A form of human carboxypeptidase has been isolated. (nih.gov)
  • Proprotein convertases (PCs) cleave precursors after dibasic residues, and carboxypeptidases remove basic residues from the C terminals. (jneurosci.org)
  • Two critical processing steps are proteolytic cleavage after dibasic residues by proprotein convertases (PCs) and removal of the dibasic residues from the C terminals of the cleaved peptides by carboxypeptidases. (jneurosci.org)
  • Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. (prospecbio.com)
  • Carboxypeptidase-B sequentially cleaves C-terminal K and R residues. (biovendor.com)
  • Carboxypeptidases (CP), carboxypeptidase N (CPN) and carboxypeptidase R (CPR), have been reported as a protease, which can cleave carboxy-terminal arginine or lysine residues from biologically active peptides, such as C3a and C5a, and regulate their activity. (biomedcentral.com)
  • Carboxypeptidase A usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side chains. (chemeurope.com)
  • Background Removal of C-terminal lysine residues that are continuously exposed in lysing fibrin is an established anti-fibrinolytic mechanism dependent on the plasma carboxypeptidase TAFIa, which also removes arginines that are exposed at the time of fibrinogen clotting by thrombin. (elsevier.com)
  • Carboxypeptidases are proteases that hydrolyze the peptide bonds at the carboxy-terminal end of a chain of amino acids and have been identified in a wide variety of cell types and animals. (google.com)
  • Activation peptide of carboxypeptidase B and anionic trypsinogen as early predictors of the severity of acute pancreatitis. (thefreedictionary.com)
  • Methotrexate-α-phenylalanine (MTX-Phe), a second-generation prodrug in the MTX α-peptide series designed for activation to MTX by carboxypeptidase-mAb conjugates, was synthesized by reaction of the p -nitrophenyl ester of 4-amino-4-deoxy-10-methylpteroic acid with l -glutamyl-α- l -phenylalanine. (aacrjournals.org)
  • The insulin-secretory-granule carboxypeptidase shared several properties of carboxypeptidase H from bovine adrenal medulla and pituitary. (portlandpress.com)
  • amino acids with similar specificity as observed for the human pancreatic juice, whereas bovine carboxypeptidase B cleaved the basic amino acid conjugates. (eurekamag.com)
  • SNP detection of carboxypeptidase E gene and its association with meat quality and carcass traits in Korean cattle. (thefreedictionary.com)
  • This is the first report of a serine carboxypeptidase-like gene induced by gibberellins in reproductive and vegetative developing tissues in dicotyledoneous plants. (deepdyve.com)
  • 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. (nih.gov)
  • Two independent mutants of Escherichia coli deficient in dipeptidyl carboxypeptidase activity (Dep-) were isolated after mutagenesis with ethyl methanesulfonate. (pnas.org)
  • Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli . (springer.com)
  • Chowdhury C, Nayak TR, Young KD et al (2010) A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli . (springer.com)
  • Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. (harvard.edu)
  • CPB2 is activated by trypsin and acts on carboxypeptidase B substrates. (thermofisher.com)
  • Plasma levels of carboxypeptidase U (CPU, CPB2 or TAFIa) are elevated in patients with acute myocardial infarction. (nih.gov)
  • Recommend recombinant carboxypeptidase B lyophilized should be stored under 2-8℃ in sealed container. (polstate.com)
  • Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. (polstate.com)
  • Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI). (semanticscholar.org)
  • Generated stable deletion mutant of TAFI with full carboxypeptidase activity without activation. (nih.gov)
  • Carboxypeptidase A2 ( CPA2 ) is a secreted pancreatic procarboxy -peptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. (sinobiological.com)
  • YaxinBio is specialized in the research and the production of Animal Origin Free recombinant carboxypeptidase B and recombinant trypsin, which are of high importance for the production of human recombinant insulin. (thefreedictionary.com)
  • Bioinformatics analysis revealed an additional 49 β-lybatide-like plant carboxypeptidase inhibitors. (ntu.edu.sg)
  • Objective To evaluate the impact of alterations in fibrin structure mediated by constitutive carboxypeptidase activity on the function of fibrin as a template for tissue plasminogen activator-(tPA) induced plasminogen activation and its susceptibility to digestion by plasmin. (elsevier.com)
  • Sun L, Guo C, Burnett J, Pan J, Yang Z, Ran Y, Sun D. Association between expression of Carboxypeptidase 4 and stem cell markers and their clinical significance in liver cancer development. (jcancer.org)
  • This study aimed to evaluate the expression of carboxypeptidase 4 (CPA4) in hepatitis, liver cirrhosis and liver cancer tissues, and revealed its clinical significance in liver cancer progression. (jcancer.org)
  • A novel subfamily of mouse cytosolic carboxypeptidases. (ebi.ac.uk)
  • Loss of prolyl carboxypeptidase in two-kidney, one-clip goldblatt hypertensive mice. (harvard.edu)
  • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. (semanticscholar.org)
  • Carboxypeptidases that cleave positively charged amino acids (arginine, lysine) are called carboxypeptidase B (B for basic). (wikipedia.org)
  • Cholyl-L-lysine and cholyl-L-arginine were also cleaved by serum and plasma, which are known to possess carboxypeptidase activity. (eurekamag.com)
  • Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. (creative-enzymes.com)
  • Carboxypeptidase B is competitively inhibited by arginine and lysine. (polstate.com)
  • The fact that two of the least related proteins within this clade are acyltransferases rather than true serine carboxypeptidases suggests that some or all of the remaining members of this group may have similar activities. (plantphysiol.org)
  • Aspartic protease, [beta]-galactosidase, peroxidase and serine carboxypeptidase were detected in three Ephedra species. (thefreedictionary.com)
  • CPA (carboxypeptidase A) is another MC protease, co-localized with chymase in severe atherosclerotic lesions. (portlandpress.com)
  • Carboxypeptidase A4 (CPA4) is an extracellular metallocarboxypeptidase, which was closely associated with aggressiveness. (medsci.org)
  • These experiments indicate that glycine and taurine amidates of cholic acid differ from a number of other conjugates with neutral and basic amino acid in being resistant to hydrolysis by pancreatic and plasma carboxypeptidases. (eurekamag.com)
  • Your search returned 53 carboxypeptidase A4 ELISA ELISA Kit across 8 suppliers. (biocompare.com)
  • Your search returned 24 carboxypeptidase, vitellogenic like ELISA ELISA Kit across 3 suppliers. (biocompare.com)
  • NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway. (nih.gov)
  • Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. (harvard.edu)
  • Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis. (semanticscholar.org)
  • Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. (ebi.ac.uk)
  • Methods and results We used the stable carboxypeptidase B (CPB), which shows the same substrate specificity as TAFIa. (elsevier.com)
  • 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. (nih.gov)
  • A genomic clone for human carboxypeptidase has been isolated with a probe for rat CPA1 cDNA. (nih.gov)
  • Carbonell, Juan 2004-10-17 00:00:00 A cDNA clone encoding a serine carboxypeptidase (PsCP), isolated from young fruits of Pisum sativum L., was used to study the temporal and spatial expression and hormonal regulation of serine carboxypeptidase during reproductive and vegetative development. (deepdyve.com)
  • PBPs are also involved in PG remodeling by catalyzing DD-carboxypeptidase (DD-CPase) and endopeptidase reactions. (springer.com)
  • One Unit of carboxypeptidase B activity hydrolyzes one micromole of hippuryl-L-arginine per minute at 25℃, pH 7.65. (polstate.com)
  • Vancomycin and ristocetin are shown to inhibit the hydrolysis of sensitive peptides by the Streptomyces albus G D-alanyl-D carboxypeptidase and the mechanism of inhibition is discussed. (ac.be)
  • In this classification system, carboxypeptidases that have a stronger preference for those amino acids containing aromatic or branched hydrocarbon chains are called carboxypeptidase A (A for aromatic/aliphatic). (wikipedia.org)

Xaa = any amino acid residue
↓ = cleavage site
XaaXaaXaaXaaXaaXaanot Ser