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 3.4.2.1 and EC 3.4.12.2.
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.
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 3.4.2.2 and EC 3.4.12.3.
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 carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.
A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on GAMMA-AMINOBUTYRIC ACID mediated synaptic transmission.
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.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
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 subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The rate dynamics in chemical or physical systems.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
The process of cleaving a chemical compound by the addition of a molecule of water.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The sum of the weight of all the atoms in a molecule.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae. (1/264)

To date zinc carboxypeptidases have only been found in animals and actinomycete bacteria. A cDNA clone (MeCPA) for a novel fungal (Metarhizium anisopliae) carboxypeptidase (MeCPA) was obtained by using reverse transcription differential display polymerase chain reaction to identify pathogenicity genes. MeCPA resembles pancreatic carboxypeptidases in being synthesized as a precursor species (418 amino acids) containing a large amino-terminal fragment (99 amino acids). The mature (secreted) form of MeCPA shows closest amino acid identity to human carboxypeptidases A1 (35%) and A2 (37%). MeCPA was expressed in an insect cell line yielding an enzyme with dual A1 + A2 specificity for branched aliphatic and aromatic COOH-terminal amino acids. However, in contrast to the very broad spectrum A + B-type bacterial enzymes, MeCPA lacks B-type activity against charged amino acids. This is predictable as key catalytic residues determining the specificity of MeCPA are conserved with those of mammalian A-type carboxypeptidases. Thus, in evolutionary terms the fungal enzyme is an intermediate between the divergence of A and B forms and the differentiation of the A form into A1 and A2 isoforms. Ultrastructural immunocytochemistry of infected host (Manduca sexta) cuticle demonstrated that MeCPA participates with the concurrently produced endoproteases in procuring nutrients; an equivalent function to digestive pancreatic enzymes.  (+info)

Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1. (2/264)

A full-length cDNA clone coding for porcine pancreatic preprocarboxypeptidase A1 (prePCPA1) was isolated from a cDNA library. The open reading frame (ORF) of the nucleotide sequence was 1260 nt in length and encoded a protein of 419 amino acids (aa). The cDNA included a short signal peptide of 16 aa and a 94 aa-long activation segment. The calculated molecular mass of the mature proenzyme was 45561 Da, in accordance with that of the purified porcine pancreatic PCPA1. The deduced aa sequence of the corresponding enzyme differed from that predicted by the three-dimensional structure by 40 aa, and showed 85% identity and 55% identity to that of procarboxypeptidases A1 and A2, respectively. Moreover the sequence was identical to that of several independent cDNA clones, suggesting that it is the major transcribed gene. No evidence for a second variant was observed in the cDNA library and PCPA2 is apparently absent from the porcine pancreas. The cDNA was expressed in Saccharomyces cerevisiae under the control of the yeast triose phosphate isomerase promoter. The signal peptide of the PCPA protein efficiently directed its secretion into the culture medium (1.5 mg.L-1) as a protein of the predicted size. The recombinant proenzyme was analyzed by immunological and enzymological methods. Its activation behavior was comparable with that of the native form and led to a 35-kDa active enzyme.  (+info)

Effect of self-association of alphas1-casein and its cleavage fractions alphas1-casein(136-196) and alphas1-casein(1-197),1 on aromatic circular dichroic spectra: comparison with predicted models. (3/264)

The self-association of native alphas1-casein is driven by a sum of interactions which are both electrostatic and hydrophobic in nature. The dichroism of aromatic side chains was used to derive regio-specific evidence in relation to potential sites of alphas1-casein polymerization. Near-ultraviolet circular dichroism (CD) revealed that both tyrosine and tryptophan side chains play a role in alphas1-casein associations. Spectral evidence shows these side chains to be in an increasingly nonaqueous environment as both ionic strength and protein concentration lead to increases in the degree of self-association of the protein from dimer to higher oligomers. Near-UV CD investigation of the carboxypeptidase A treated peptide, alphas1-casein(1-197), indicated that the C-terminal residue (Trp199) may be superficial to these interactions, and that the region surrounding Trp164 is more directly involved in an aggregation site. Similar results for the cyanogen bromide cleavage peptide alphas1-casein(136-196) indicated the presence of strongly hydrophobic interactions. Association constants for the peptides of interest were determined by analytical ultracentrifugation, and also were approximated from changes in the near-UV CD curves with protein concentration. Sedimentation equilibrium experiments suggest the peptide to be dimeric at low ionic strength; like the parent protein, the peptide further polymerizes at elevated (0.224 M) ionic strength. The initial site of dimerization is suggested to be the tyrosine-rich area near Pro147, while the hydrophobic region around Pro168, containing Trp164, may be more significant in the formation of higher-order aggregates.  (+info)

Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. (4/264)

Butyrate and its structural analogues have recently entered clinical trials as a potential drug for differentiation therapy of advanced prostate cancer. To better understand the molecular mechanism(s) involved in prostate cancer differentiation, we used mRNA differential display to identify the gene(s) induced by butyrate. We found that the androgen-independent prostate cancer cell line PC-3 undergoes terminal differentiation and apoptosis after treatment with sodium butyrate (NaBu). A novel cDNA designated carboxypeptidase A3 (CPA3), which was up-regulated in NaBu-treated PC-3 cells, was identified and characterized. This gene expresses a 2795-bp mRNA encoding a protein with an open reading frame of 421 amino acids. CPA3 has 37-63% amino acid identity with zinc CPs from different mammalian species. It also shares 27-43% amino acid similarity with zinc CPs from several nonmammalian species, including Escherichia coli, yeast, Caenorhabditis elegans, and Drosophila. The structural similarity between CPA3 and its closest homologues indicates that the putative CPA3 protein contains a 16-residue signal peptide sequence, a 95-residue NH2-terminal activation segment, and a 310-residue CP enzyme domain. The consistent induction of CPA3 by NaBu in several prostate cancer cell lines led us to investigate the signaling pathway involved in the induction of CPA3 mRNA. Trichostatin A, a potent and specific inhibitor of histone deacetylase, also induced CPA3 mRNA expression, suggesting that CPA3 gene induction is mediated by histone hyperacetylation. We demonstrated that CPA3 induction was a downstream effect of the treatment with butyrate or trichostatin A, but that the induction of p21(WAF1/CIP1) occurred immediately after these treatments. We also demonstrated that the induction of CPA3 mRNA by NaBu was inhibited by p21(WAF1/CIP1) antisense mRNA expression, indicating that p21 transactivation is required for the induction of CPA3 by NaBu. Our data demonstrate that the histone hyperacetylation signaling pathway is activated during NaBu-mediated differentiation of PC-3 cells, and the new gene, CPA3, is involved in this pathway.  (+info)

A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. (5/264)

The first gene of a family of prokaryotic proteases with a specificity for L,D-configured peptide bonds has been identified in Escherichia coli. The gene named ldcA encodes a cytoplasmic L, D-carboxypeptidase, which releases the terminal D-alanine from L-alanyl-D-glutamyl-meso-diaminopimelyl-D-alanine containing turnover products of the cell wall polymer murein. This reaction turned out to be essential for survival, since disruption of the gene results in bacteriolysis during the stationary growth phase. Owing to a defect in muropeptide recycling the unusual murein precursor uridine 5'-pyrophosphoryl N-acetylmuramyl-tetrapeptide accumulates in the mutant. The dramatic decrease observed in overall cross-linkage of the murein is explained by the increased incorporation of tetrapeptide precursors. They can only function as acceptors and not as donors in the crucial cross-linking reaction. It is concluded that murein recycling is a promising target for novel antibacterial agents.  (+info)

Albumin banks peninsula: a new termination variant characterised by electrospray mass spectrometry. (6/264)

Albumin Banks Peninsula is an electrophoretically fast variant that is expressed at only 2% of the total serum albumin. Electrospray ionisation analysis indicated a mass decrease of 755 Da relative to normal albumin and carboxypeptidase A digestion, together with CNBr peptide mapping, indicated a C-terminal truncation. This was confirmed by PCR and DNA sequence analysis which showed the introduction of a new AG acceptor splice site near the 3' end of intron 13. Predictably this results in the replacement of the C-terminal GKKLVAASQAALGL sequence by SLCSG and would be associated with an 861 Da decrease in molecular mass. We surmised that the new Cys was most probably cysteinylated as this albumin species would have a mass decrease of 742 Da and be very close to the measured value of 755 Da. Cysteinylation was confirmed when a mass decrease of 863 Da was measured between the proteins after reduction of their disulfide bonds.  (+info)

Enhancement of heparin cofactor II anticoagulant activity. (7/264)

Heparin cofactor II (HCII) is a serpin whose thrombin inhibition activity is accelerated by glycosaminoglycans. We describe the novel properties of a carboxyl-terminal histidine-tagged recombinant HCII (rHCII-CHis(6)). Thrombin inhibition by rHCII-CHis(6) was increased >2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin. Enhanced activity of rHCII-CHis(6) was reversed by treatment with carboxypeptidase A. We assessed the role of the HCII acidic domain by constructing amino-terminal deletion mutants (Delta1-52, Delta1-68, and Delta1-75) in wt-rHCII and rHCII-CHis(6). Without glycosaminoglycan, unlike wt-rHCII deletion mutants, the rHCII-CHis(6) deletion mutants were less active compared with full-length rHCII-CHis(6). With glycosaminoglycans, Delta1-68 and Delta1-75 rHCIIs were all less active. We assessed the character of the tag by comparing rHCII-CHis(6), rHCII-CAla(6), and rHCII-CLys(6) to wt-rHCII. Only rHCII-CHis(6) had increased activity with heparin, whereas all three mutants have increased heparin binding. We generated a carboxyl-terminal histidine-tagged recombinant antithrombin III to study the tag on another serpin. Interestingly, this mutant antithrombin III had reduced heparin cofactor activity compared with wild-type protein. In a plasma-based assay, the glycosaminoglycan-dependent inhibition of thrombin by rHCII-CHis(6) was significantly greater compared with wt-rHCII. Thus, HCII variants with increased function, such as rHCII-CHis(6), may offer novel reagents for clinical application.  (+info)

2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1, 5-bisphosphate carboxylase/oxygenase against proteolytic breakdown. (8/264)

Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2'-carboxy-D-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg2+ and CO2. CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO2 assimilation. Rubisco turnover (in the presence of RuBP, Mg2+ and CO2) may confer similar protection against proteases in the light.  (+info)

Carboxypeptidase A (CPA) is a pancreatic exopeptidase which hydrolyses the peptide bond adjacent to the C-terminal end in polypeptide chains. Mast cell carboxypeptidase A (MC-CPA), a part of the peptidase M14 family, is a highly conserved metalloprotease localized to the secretory granules, along with trytases and chymases. MC-CPA is stored as an active enzyme in the granule and is released, along with other inflammatory mediators, upon mast cell degranulation. MC-CPA mirrors pancreatic carboxypeptidase A in cleaving COOH-terminal aromatic and aliphatic amino acid residues. The optimum pH of MC-CPA is between neutral and basic, depending upon the substrate. The MC-CPA gene, CPA3, resides on chromosome 3 and contains 11 exons ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Recombinant Rat Carboxypeptidase A protein (Tagged) is an Escherichia coli Full length protein 111 to 419 aa range, | 85% purity and validated in SDS-PAGE.
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The immersed boundary-lattice Boltzmann method was presented recently to simulate the rigid particle motion. It combines the desirable features of the lattice Boltzmann and immersed boundary methods. It uses a regular Eulerian grid for the flow domain and a Lagrangian grid for the boundary. For the lattice Boltzmann method, as compared with the single-relaxation-time collision scheme, the multi-relaxation-time collision scheme has better computational stability due to separation of the relaxations of various kinetic models, especially near the geometric singularity. So the multi-relaxation-time collision scheme is used to replace the single-relaxation-time collision scheme in the original immersed boundary-lattice Boltzmann method. In order to obtain an accurate result, very fine lattice grid is needed near the solid boundary. To reduce the computational effort, local grid refinement is adopted to offer high resolution near a solid body and to place the outer boundary far away from the body. So ...
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We acknowledge financial support from the University of Warwick and the China Scholarship Council. Equipment used in this research was funded by the Innovative Uses for Advanced Materials in the Modern World (AM2) with support from AWM and ERDF. D.M.H. is a Royal Society/Wolfson Fellow and C.R.B. is a Science City Senior Research Fellow. Dr. Christopher N. Scanlan has provided the gp120.. ...
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.
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The coefficients plot above indicates which X-variables have the most overall impact on the Y-variables (product quality). Each bar represents one particular X-variable. The X-variables are colour-coded according to 4 defined blocks of data. Here, it is readily observed that the orange block (Raw Materials & Blending Ratios) and green block (Properties of Raw Materials) have the most significant impact on product quality in the MVA multi-block model. Further, the purple block (Analytical Tests) provide little value, suggesting that consideration could be made to eliminate these tests and their associated costs. ...
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Enrique Santos-Bueso, Federico Sáenz-Francés, Mercedes Serrador-García, Jesús Porta-Etessam, José María Martínez-de-la-Casa, Julián García-Feijoo, Julián García-Sánchez Eur J Ophthalmol 2014; 24(6): 960 - 963 ...
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Formed from pig chymotrypsinogen C, and from cattle subunit II of procarboxypeptidase A. Reacts more readily with Tos-Leu-CH2Cl than Tos-Phe-CH2Cl in contrast to chymotry
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A much *simplified* example on how I teach this stuff... Lets say we have a table that has 10,000,000 rows which are stored in 1,000,000 data blocks meaning we have approximately 10 rows per block on average. Lets say we have an index on this table that has 100,000 leaf blocks meaning we have on average approximately 100 leaf entries per leaf block the index has 3 levels. Lets also say we have an effective multi-block read capability of 10 blocks per I/O (meaning Oracle will read 10 consecutive blocks at a time on average during a full table scan multiblock read). Finally, lets say were interested in accessing *just* 10% of the data (or 1,000,000 of the total 10,000,000 rows). Will Oracle use the index or wont it ? Hopefully, Ive picked an easy set of numbers to help illustrate the answer ... Firstly, to calculate the cost of using the index access path. We need to read the root block + a branch block in order to get to the first leaf block of interest. Thats 2 logical I/Os (LIOs). ...
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Introdução: O câncer de mama é a neoplasia mais freqüente e também a principal causa de morte por câncer entre as mulheres. O gene TP53 é polimórfico no códon 72 da proteína que ele codifica, podendo conter arginina (CGC) ou prolina (CCC) nesta posição. Este polimorfismo pode estar envolvido na suscetibilidade e predisposição ao câncer e apresenta uma distribuição étnica e geográfica bastante variável. O genótipo homozigoto para arginina parece ser um fator de risco e prognóstico significativo para o câncer de mama. Métodos: Extraído DNA a partir do sangue periférico de 76 pacientes consecutivas com carcinoma ductal invasor (CDI), tratadas no Serviço de Mastologia do HCPA, em qualquer estágio da doença. 80 amostras de DNA do grupo controle de doadores saudáveis do Banco de Sangue do HCPA foram incluídas de forma aleatória. Foram coletados dados demográficos e dados das características clínicas e histopatológicas e realizada a amplificação do éxon 4 do gene ...
Introdução: As fissuras labiopalatinas são resultados de malformação decorrentes de falhas no desenvolvimento ou na maturação dos processos embrionários. Objetivo: descrever os achados audiológicos em crianças com FLP, atendidas no centro de otite média do Brasil do HCPA. Métodos: A população foi composta de crianças portadoras de FLP atendidas no centro de otite média do Brasil do HCPA no período de 2007 a 2009, 55 do gênero feminino e 51 masculino, com idades entre quatro a 10 anos. Todas realizaram avaliação otorrinolaringológica e audiometria tonal. Resultados: A amostra foi composta de 106 com média de 6,2 anos (± 1,3), predominância foi sexo feminino (n=55;51%). Quando comparados os limiares das orelhas direita e esquerda houve uma diferença significativa na frequência 250Hz, na pesquisa da via aérea (p,0,001). Os valores foram mais elevados na orelha direita. Encontramos em nosso estudo um total (63%) limiares auditivos normais, (42%) perda auditiva condutiva ...
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Weinert, Letícia Schwerz; Triches, Cristina Bergmann; Leitão, Cristiane Bauermann; Miltersteiner, Diego; Costa, Cezar Amauri Ribeiro da; Balbinotto, Antônio; Silveiro, Sandra Pinho; Gross, Jorge Luiz (HCPA/FAMED/UFRGS, 2007) ...
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Your performance during the CPA examination is final and not subject to revision. CPA examination strategies that maximize your CPA-Exam-taking efficiency are
CPA vs Accountant CPA or Certified Public Accountant and Accountant perform almost the same duties. But the fact is that all accountants cannot be Certified
Пластырь от варикоза является современным средством, которое работает по всем трем направлениям. В его состав входят 10 мощнейших лекарственных растений. Они не одно тысячелетие использовались на Тибете и в Китае, а сегодня их целебные эффекты доказаны учеными.. ...
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 ...
TY - JOUR. T1 - The activation pathway of procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic processing. AU - Villegas, Virtudes. AU - Vendrell, Josep. AU - Avilés, Francesc X.. PY - 1995/1/1. Y1 - 1995/1/1. N2 - The activation process of porcine pancreatic procarboxypeptidase B (pro‐CPB) has been studied in detail by a number of complementary methodologies, and a description of the molecular events that lead to the generation of active carboxypeptidase B (CPB) has been deduced. The generated CPB participates in the degradation of its own activation segment by excising C‐terminal residues from fragments produced by tryptic proteolysis. The trimming action of CPB is, however, not essential for the release of a fully functional enzyme, in contrast to what was previously reported for porcine procarboxypeptidase A (pro‐CPA). In the model presented here, the activation process is solely dependent on the first tryptic cleavage, at the limit ...
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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 ...
Extensive genetic studies of chronic pancreatitis over the past decade have highlighted the importance of a tightly regulated balance between activation and inactivation of trypsin within the pancreas to disease susceptibility and resistance. The recent identification of chymotrypsin C (CTRC) as enz …
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013 ...
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Structure of the carboxypeptidase b complex with n-sulfamoyl-l-phenylalanine - a transition state analog of non-specific substrate / V. Akparov, V. Timofeev, I. Khaliullin et al. // Journal of Biomolecular Structure and Dynamics, издательство Taylor & Francis. - 2017. Carboxypeptidase B (EC 3.4.17.2) (CPB) is commonly used in the industrial insulin production and as a template for drug design. However, its ability to discriminate substrates with hydrophobic, hydrophilic, and charged side chains is not well understood. We report structure of CPB complex with a transition state analog N-sulfamoyl-L-phenylalanine solved at 1.74Å. The study provided an insight into structural basis of CPB substrate specificity. Ligand binding is affected by structure-depended conformational changes of Asp255 in S1-subsite, interactions with Asn144 and Arg145 in C-terminal binding subsite, and Glu270 in the catalytic center. Side chain of the non-specific substrate analog SPhe in comparison with that of ...
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 ...
Probable carboxypeptidase X1 is an enzyme that in humans is encoded by the CPXM1 gene. The protein encoded by this gene is a member of the M14 family of zinc carboxypeptidases; however, the protein has no detectable carboxypeptidase activity. The encoded protein is thought to be an extracellular and/or membrane protein, and may be involved in cell-cell interactions. GRCh38: Ensembl release 89: ENSG00000088882 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027408 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta ...
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Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
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Reeck, G.R., Walsh, K.A. and Neurath, H. (1971). „Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry. 10: 4690-4698. PMID 5140186 ...
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Enzymes: strong secretion of amylases (α-amylase and glucoamylase); some carboxypeptidase; low tyrosinase ...
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. ...
Carboxypeptidase, which is a protease that takes off the terminal amino acid group from a protein ...
CPN2: Carboxypeptidase N subunit 2. *CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental ...
Wang T, Parris J, Li L, Morgan JI (2006). "The carboxypeptidase-like substrate-binding site in Nna1 is essential for the rescue ... ATP/GTP binding protein 1 is gene that encodes the protein known as cytosolic carboxypeptidase 1 (CCP1), originally named NNA1 ... CCP1/NNA1 is a zinc carboxypeptidase that contains nuclear localization signals that was initially cloned from regenerating ... with alleles containing a zinc carboxypeptidase domain and an ATP/GTP binding motif, a protein first identified in alpha- ...
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 ...
SCPEP1: encoding enzyme Retinoid-inducible serine carboxypeptidase. *SEBOX: encoding protein SEBOX homeobox ...
Psi-loop motif from Carboxypeptidase A. Psi-loop motif[edit]. The psi-loop (Ψ-loop) motif consists of two antiparallel strands ...
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 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 3.4.15.5, 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 ...
Carboxypeptidase, a hydrolytic enzyme important in digestion. Another complex ion enzyme is catalase, which decomposes the ...
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 ...
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, ...
"Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation". Science. 358 (6369): 1448-1453. ...
... procollagen carboxypeptidase; procollagen carboxy-terminal proteinase; procollagen peptidase, BMP-1, EC 3.4.24.19) merupakan ...
... 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: ...
However, carboxypeptidases do not have something similar to the C-domain. In carboxypeptidase A, the active site is accessible ...
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 ...
Carboxypeptidase T (EC 3.4.17.18, 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- ...
... 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 ...
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 3.4.17.14, 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". ...
... carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme. ... Muramoyltetrapeptide+carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... Metz R, Henning S, Hammes WP (March 1986). "LD-carboxypeptidase activity in Escherichia coli. II. Isolation, purification and ... DasGupta H, Fan DP (July 1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium ...
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 ...
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 ...
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 ...
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 ...
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 3.4.15.1 ...
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 ...
Similar to that of carboxypeptidase A EC 3.4.17.1, 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 ...
Loss of prolyl carboxypeptidase in two-kidney, one-clip goldblatt hypertensive mice. PLoS One. 2015; 10(2):e0117899. ... "Carboxypeptidases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... A D, D-carboxypeptidase is required for Vibrio cholerae halotolerance. Environ Microbiol. 2015 Feb; 17(2):527-40. ... Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. Mol Biol Cell. 2014 ...
Lysosomal protective protein, EC 3.4.16.5 (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 3.4.17.21) 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 ...
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 3.4.17.12 lysate ...
Browse our Carboxypeptidase M Protein catalog backed by our Guarantee+. ... Carboxypeptidase M Proteins. We offer Carboxypeptidase M Peptides and Carboxypeptidase M Proteins for use in common research ... Our Carboxypeptidase M Peptides and Carboxypeptidase M Proteins can be used in a variety of model species: Human. Use the list ... Each Carboxypeptidase M Peptide and Carboxypeptidase M Protein is fully covered by our Guarantee+, to give you complete peace ...
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 T ( EC 3.4.17.18 , CPT ) is an enzyme . (wikipedia.org)
  • Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14, 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)
  • Muramoyltetrapeptide carboxypeptidase (EC 3.4.17.13, carboxypeptidase IIW, carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme. (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 3.4.15.1). (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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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 3.4.17.2), 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 3.4.17.21) - 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 3.4.17.21) 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 3.4.17.21) 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 3.4.17.21) 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 3.4.17.21) 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 3.4.17.21). (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)
  • Membrane-bound carboxypeptidase (CP) M is an important regulator of the kallikrein- kinin system via its ability to generate des-Arg-kinin agonists of the G-protein coupled kinin B1 receptor (B1R). (grantome.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)
  • 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)
  • 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)
  • 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)
  • LD-carboxypeptidase activity in Escherichia coli. (wikipedia.org)
  • 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)
  • 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)
  • Carboxypeptidase G2 (CPG2) Inhibitor is a novel Carboxypeptidase G2 (CPG2) Inhibitor, Antitumor agents. (adooq.com)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • Carboxypeptidase A usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side chains. (chemeurope.com)
  • 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)
  • 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 3.4.17.1 , 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-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)
  • 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)
  • 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)
  • 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)
  • The novel human proteins (NHPs) described for the first time herein share structural similarity with animal proteases, and especially carboxypeptidases. (google.com)
  • The carboxypeptidase A family can be divided into four subfamilies: M14A (carboxypeptidase A or digestive), M14B (carboxypeptidase H or regulatory), M14C (gamma-D-glutamyl-L-diamino acid peptidase I) and M14D (AGTPBP-1/Nna1-like proteins) [ PMID: 7674922 , PMID: 17244818 ]. (ebi.ac.uk)
  • Hayashi, R., Moore, S., and Stein, W. H. (1973) Carboxypeptidase from yeast:Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. (springer.com)
  • Our Carboxypeptidase M Peptides and Carboxypeptidase M Proteins can be used in a variety of model species: Human. (novusbio.com)
  • Choose from our Carboxypeptidase M Peptides and Proteins. (novusbio.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)
  • We are investigating the interaction of two proteins, carboxypeptidase M and B1 receptor, on the cell surface that results in increased production of regulatory molecules that affect cell and organ function. (grantome.com)
  • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. (semanticscholar.org)
  • Pro-(carboxypeptidases A) from whole pig pancreas. (biochemj.org)
  • Sedimentation analysis and light-scattering measurements were made with the two forms of pig pancreas pro-(carboxypeptidase A), in order to determine some of their physical properties. (biochemj.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 complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". Eur. (wikipedia.org)
  • 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)
  • Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. (abcam.com)
  • 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)
  • 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)
  • 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)
  • 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)
  • Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. (harvard.edu)
  • NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway. (nih.gov)
  • 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)
  • 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 paper we link the catalytic activity of carboxypeptidase N to tumor progression in clinical samples from breast cancer patients and a breast cancer animal model. (thefreedictionary.com)
  • On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B. (semanticscholar.org)
  • coli , most LMM PBP exhibit dd-carboxypeptidase activity, are not essential for growth in routine laboratory media, and contributions to virulent phenotypes remain largely unknown. (bioportfolio.com)
  • en] The activity of the D-alanyl-D carboxypeptidase from the penicillin-resistant Streptomyces albus G is not or very little affected by penicillins and related antibiotics. (ac.be)
  • Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with transcriptional repression function: stimulation of enzymic activity by its target DNA. (sickkids.ca)

Xaa = any amino acid residue
↓ = cleavage site
P6P5P4P3P2P1P1′
XaaXaaXaaXaaXaaXaanot Ser