Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Carboxypeptidases A: 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.Lysine Carboxypeptidase: 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.Carboxypeptidase B: 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.Carboxypeptidase H: 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.Cathepsin A: 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.Penicillin G: 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.Amino Acid Sequence: 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.Molecular Sequence Data: 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Amino Acids: 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.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Kinetics: The rate dynamics in chemical or physical systems.Pancreas: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Cloning, Molecular: 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.Chymotrypsin: 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.Trypsin: 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.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Hydrogen-Ion Concentration: 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)Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Peptides: 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.Sequence Alignment: 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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cattle: 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.Protein Conformation: 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).Micromonosporaceae: A family of gram-positive, saprophytic bacteria occurring in soil and aquatic environments.Thermoactinomyces: A genus of gram-positive bacteria in the family Thermoactinomycetaceae, that can cause FARMER'S LUNG.Encyclopedias as Topic: 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)Micromonospora: A genus of gram-positive bacteria that forms a branched mycelium. It commonly occurs as a saprophytic form in soil and aquatic environments.Serine-Type D-Ala-D-Ala Carboxypeptidase: 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.Streptomyces: 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.Dictionaries, MedicalDictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.Protein O-Methyltransferase: 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.-.Polynucleotide 5'-Hydroxyl-Kinase: An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.Polyribonucleotide Nucleotidyltransferase: 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 2.7.7.8.PolynucleotidesPatents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Exoribonucleases: 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.-Sodium Azide: A cytochrome oxidase inhibitor which is a nitridizing agent and an inhibitor of terminal oxidation. (From Merck Index, 12th ed)Antibodies: 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).Books, Illustrated: 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)Abstracting and Indexing as Topic: Activities performed to identify concepts and aspects of published information and research reports.Antibody Specificity: 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, Monoclonal: Antibodies produced by a single clone of cells.Rabbits: 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.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (1/1719)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

A soluble form of the avian hepatitis B virus receptor. Biochemical characterization and functional analysis of the receptor ligand complex. (2/1719)

Avian hepatitis B virus infection is initiated by the specific interaction of the extracellular preS part of the large viral envelope protein with carboxypeptidase D (gp180), the primary cellular receptor. To functionally and biochemically characterize this interaction, we purified a soluble form of duck carboxypeptidase D from a baculovirus expression system, confirmed its receptor function, and investigated the contribution of different preS sequence elements to receptor binding by surface plasmon resonance analysis. We found that preS binds duck carboxypeptidase D with a 1:1 stoichiometry, thereby inducing conformational changes but not oligomerization. The association constant of the complex was determined to be 2.2 x 10(7) M-1 at 37 degreesC, pH 7.4, with an association rate of 4.0 x 10(4) M-1 s-1 and a dissociation rate of 1.9 x 10(-3) s-1, substantiating high affinity interaction of avihepadnaviruses with their receptor carboxypeptidase D. The separately expressed receptor-binding domain, comprising about 50% of preS as defined by mutational analysis, exhibits similar constants. The domain consists of an essential element, probably responsible for the initial receptor contact and a part that contributes to complex stabilization in a conformation sensitive manner. Together with previous results from cell biological studies these data provide new insights into the initial step of hepadnaviral infection.  (+info)

Properties of non-polymerizable tropomyosin obtained by carboxypeptidase A digestion. (3/1719)

Tropomyosin digested with carboxypeptidase A [EC 3.4.12.2] (CTM) shows a lower viscosity than the undigested protein in solution. From the relation between the viscosity decrease and the amount of amino acids liberated from the carboxyl terminus during this digestion, it is inferred that loss of the tri-peptide-Thr-Ser-Ile from the C-terminus is responsible for the decrease in viscosity. The secondary structure of -TM was not affected by the digestion according to circular dichroic measurements. The viscosity of CTM did not increase in methanol-water mixtures, whereas that of tropomyosin increased markedly. These results indicate that polymerizability was lost upon the removal of a small peptide from the C-terminus without change in the secondary structure. A decrease in the viscosity of tropomyosin solutions was observed on the addition of CTM, indicating that CTM interacts with intact tropomyosin. The dependence of the viscosity decrease on the amount of CTM showed that CTM binds tropomyosin in a one-to-one ratio as a result of end-to-end interaction. Since paracrystals having a 400 A repeated band structure could be grown in the presence of Mg ions at neutral pH, side-by-side interactions in CTM molecules remain intact, even though polymerizability is lost. The disc gel electrophoretic pattern showed that troponin could bind to CTM, but no increase in viscosity due to the complex was observed in solution. That is, the C-terminal part of tropomyosin is not required for the formation of the complex. The amount of CTM bound to F-actin was less than half of that bound to undigested tropomyosin, and could be reduced to one-tenth by a washing procedure. In the presence of troponin, however, the amount recovered to the level of tropomyosin normally bound to F-actin. Therefore, it is concluded that troponin is bound in the middle of the tropomyosin molecule and strengthens the binding of tropomyosin to F-actin.  (+info)

Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY. (4/1719)

BACKGROUND: Vancomycin-resistant enterococci are pathogenic bacteria that attenuate antibiotic sensitivity by producing peptidoglycan precursors that terminate in D-Ala-D-lactate rather than D-Ala-D-Ala. A key enzyme in effecting antibiotic resistance is the metallodipeptidase VanX, which reduces the cellular pool of the D-Ala-D-Ala dipeptide. RESULTS: We constructed eleven mutants, using the recently determined VanX structure as a basis, to investigate residue function. Mutating Asp142 or Ser114 showed a large effect principally on KM, consistent with roles in recognition of the D-Ala-D-Ala termini. The drastic reduction or absence of activity in the Arg71 mutants correlates with a role in the stabilization of an anionic tetrahedral transition state. Three residues of the Escherichia coli D-Ala-D-Ala ligase (Ddl), Glu15, Ser 281 and Arg255, are similarly conserved and have equivalent functions with respect to VanX, consistent with a convergent evolution of active sites to bind D-Ala-D-Ala and lower energy barriers for formation of the tetrahedral intermediate and transition states. In the N-acyl-D-Ala-D-Ala carboxypeptidase VanY, all active-site residues are conserved (except for the two responsible for recognition of the dipeptide amino terminus). CONCLUSIONS: The mutagenesis results support structure-based functional predictions and explain why the VanX dipeptidase and Ddl ligase show narrow specificity for the D,D-dipeptide substrate. The results reveal that VanX and Ddl, two enzymes that use the same substrate but proceed in opposite directions driven by distinct cofactors (zinc versus ATP), evolved similar architectural solutions to substrate recognition and catalysis acceleration. VanY sequence analysis predicts an active site and mechanism of reaction similar to VanX.  (+info)

Isolation and expression of novel human glutamate carboxypeptidases with N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV activity. (5/1719)

Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated. The gene coding for human prostate-specific membrane antigen, a marker of prostatic carcinomas, and its rat homologue glutamate carboxypeptidase II have recently been shown to possess such NAALADase activity. In contrast, a closely related member of this gene family, rat ileal 100-kDa protein, possesses a dipeptidyl peptidase IV activity. Here, we describe the cloning of human ileal 100-kDa protein, which we have called a NAALADase- "like" (NAALADase L) peptidase based on its sequence similarity to other members of this gene family, and its inability to hydrolyze NAAG in transient transfection experiments. Furthermore, we describe the cloning of a third novel member of this gene family, NAALADase II, which codes for a type II integral membrane protein and which we have localized to chromosome 11 by fluorescent in situ hybridization analysis. Transient transfection of NAALADase II cDNA confers both NAALADase and dipeptidyl peptidase IV activity to COS cells. Expression studies using reverse transcription-polymerase chain reaction and Northern blot hybridization show that NAALADase II is highly expressed in ovary and testis as well as within discrete brain areas.  (+info)

The protein disulphide-isomerase family: unravelling a string of folds. (6/1719)

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins, including peptide binding, cell adhesion and perhaps chaperone activities. Attention is now turning to the non-redox-active domains of the PDIs, which may play an important role in all of the known activities of these proteins. Thus the presence of both redox-active and -inactive domains within these proteins portends a complexity of functions differentially accommodated by the various family members.  (+info)

Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae. (7/1719)

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. (8/1719)

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)

*Carboxypeptidase

... 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 ...

*Carboxypeptidase D

... carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine ... Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active ... Song L, Fricker LD (1995). "Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, ... Carboxypeptidase D at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ...

*Carboxypeptidase C

... (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ... Carboxypeptidase C at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme catalyses the following chemical reaction Release ...

*Carboxypeptidase A

... the zinc ion and assisted by residue Glu-270 Carboxypeptidase A inhibitor Carboxypeptidase B Carboxypeptidase Carboxypeptidase ... "Carboxypeptidase A" Acc. Chem. Res. (1989) 22: 62-69 Christianson, David et al. "Carboxypeptidase A" Acc. Chem. Res. (1989) 22 ... This property of carboxypeptidase A led to the first clause of Daniel E. Koshland, Jr.'s "induced fit" hypothesis. Several ... Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with ...

*Lysine carboxypeptidase

... (EC 3.4.17.3, carboxypeptidase N, arginine carboxypeptidase, kininase I, anaphylatoxin inactivator, ... Lysine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Plummer, T.H. Jr.; Erdös, E.G. (1981). "Human plasma carboxypeptidase N". Methods Enzymol. 80: 442-449. doi:10.1016/s0076-6879( ... Skidgel, R.A. (1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends Pharmacol. Sci. 9: 301-303. doi ...

*Carboxypeptidase M

... (EC 3.4.17.12, CPM) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of C- ... Carboxypeptidase M at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... Deddish, P.A.; Skidgel, R.A.; Erdös, E.G. (1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low ... Skidgel, R.A.; Davis, R.M.; Tan, F. (1989). "Human carboxypeptidase M. Purification and characterization of membrane-bound ...

*Carboxypeptidase B

... (EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L- ... Wallace, E.F.; Evans, C.J.; Jurik, S.M.; Mefford, I.N.; Barchas, J.D. (1982). "Carboxypeptidase B activity from adrenal medulla ... The MEROPS online database for peptidases and their inhibitors: M14.003 Carboxypeptidase B at the US National Library of ... doi:10.1016/0076-6879(70)19036-7. Brodrick, J.W.; Geokas, M.C.; Largman, C. (1976). "Human carboxypeptidase B. II. Purification ...

*Carboxypeptidase A6

Carboxypeptidase A inhibitor Carboxypeptidase GRCh38: Ensembl release 89: ENSG00000165078 - Ensembl, May 2017 GRCm38: Ensembl ... Carboxypeptidase A6 (CPA6) is an metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene. It is highly ... The protein encoded by this gene belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino ... Lyons, P. J.; Callaway, M. B.; Fricker, L. D. (2008). "Characterization of Carboxypeptidase A6, an Extracellular Matrix ...

*Carboxypeptidase B2

... (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable ... 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 ( ... "Entrez Gene: CPB2 carboxypeptidase B2 (plasma)". Bouma BN, Mosnier LO (2005). "Thrombin activatable fibrinolysis inhibitor ( ...

*Muramoyltetrapeptide carboxypeptidase

... 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) Molecular and ... Metz, R.; Henning, S.; Hammes, W.P. (1986). "LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and ... DasGupta, H.; Fan, D.P. (1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium ...

*Carboxypeptidase A2

"Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2 ... Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene. Three different forms of human pancreatic ... "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)". Pascual R, Burgos FJ, Salva M, et al. (1989). "Purification and properties ...

*Carboxypeptidase A1

... is an enzyme that in humans is encoded by the CPA1 gene. Three different forms of human pancreatic ... Carboxypeptidase A1 is a monomeric pancreatic exopeptidase. It is involved in zymogen inhibition. GRCh38: Ensembl release 89: ... Stewart EA, Craik CS, Hake L, Bowcock AM (1990). "Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter". Am. ... 1986). "Assignment of the gene for carboxypeptidase A to human chromosome 7q22----qter and to mouse chromosome 6". Hum. Genet. ...

*Muramoylpentapeptide carboxypeptidase

D-alanine carboxypeptidase I, DD-carboxypeptidase, D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanine-D ... carboxypeptidase, carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine ... Muramoylpentapeptide carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Purification and properties of two D-alanine carboxypeptidases from Escherichia coli". J. Biol. Chem. 243: 3193-3201. PMID ...

*Carboxypeptidase T

"Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal ... Carboxypeptidase T (EC 3.4.17.18, CPT) is an enzyme. This enzyme catalyses the following chemical reaction Releases a C- ... Carboxypeptidase T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281-288. doi:10.1111/j.1432- ...

*Carboxypeptidase Taq

"Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1". ... Carboxypeptidase Taq (EC 3.4.17.19) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal ... Carboxypeptidase Taq at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Lee, S.-H.; Taguchi, H.; Yoshimura, E.; Minagawa, E.; Kaminogawa, S.; Ohta, T.; Matsuzawa, H. (1994). "Carboxypeptidase Taq, a ...

*Zinc carboxypeptidase

The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A ( ... "Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family". J. ... Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended ... Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to ...

*Carboxypeptidase E

... (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is ... Carboxypeptidase Carboxypeptidase A GRCh38: Ensembl release 89: ENSG00000109472 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... fills in for carboxypeptidase E in this organism. In humans, CPE is encoded by the CPE gene. Carboxypeptidase E functions in ... Carboxypeptidase E is not found in the fruit fly (Drosophila), and another enzyme (presumably carboxypeptidase D) ...

*Alanine carboxypeptidase

... (EC 3.4.17.6, N-benzoyl-L-alanine-amidohydrolase) is an enzyme. This enzyme catalyses the following ... Alanine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ...

*Carboxypeptidase U

... (EC 3.4.17.20, arginine carboxypeptidase, carboxypeptidase R, plasma carboxypeptidase B, thrombin- ... Wang, W.; Hendriks, D.F.; Scharpé, S. (1994). "Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen ... plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U. Carboxypeptidase Eaton, D.L ... Carboxypeptidase U at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ...

*Glutamate carboxypeptidase

... (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl ... Glutamate carboxypeptidase II Goldman, P.; Levy, C.C. (1967). "Carboxypeptidase G: purification and properties". Proc. Natl. ... Glutamate carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... McCullogh, J.L.; Chabner, B.A.; Bertino, J.R. (1971). "Purification and properties of carboxypeptidase G1". J. Biol. Chem. 246 ...

*DD-carboxypeptidase

... may refer to: Muramoylpentapeptide carboxypeptidase, an enzyme Zinc D-Ala-D-Ala carboxypeptidase, an enzyme ...

*Potato carboxypeptidase inhibitor

PCI also inhibits carboxypeptidase R without affecting the activity of carboxypeptidase N in the circulation and have therefore ... May 1998). "Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor ... Potato carboxypeptidase inhibitor (PCI) is a naturally occurring protease inhibitor peptide in potatoes that can form complexes ... a Redlitz A, Tan AK, Eaton DL, Plow EF (November 1995). "Plasma carboxypeptidases as regulators of the plasminogen system". J. ...

*Carboxypeptidase A inhibitor

The structure of the complex between bovine carboxypeptidase A and the 39-amino-acid carboxypeptidase A inhibitor from potatoes ... Hass GM, Nau H, Biemann K, Grahn DT, Ericsson LH, Neurath H (March 1975). "The amino acid sequence of a carboxypeptidase ... In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well- ... Rees DC, Lipscomb WN (August 1980). "Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution". Proc ...

*Glutamate carboxypeptidase II

... (GCPII), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase ... All of which refer to the same protein glutamate carboxypeptidase II. GCPII is mainly expressed in four tissues of the body, ... and carboxypeptidase activity based on the parent tissue. The hydrolysis of NAAG by GCPII obeys Michaelis-Menten kinetics ...

*Gly-X carboxypeptidase

Gly-Xaa carboxypeptidase (EC 3.4.17.4, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast ... Gly-Xaa carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Wolf, D.H.; Ehmann, C. (1978). "Carboxypeptidase S from yeast: regulation of its activity during vegetative growth and ... carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal amino acid from a ...
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 ...
en] The simplest model for the interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics involves the three following steps: (a) the formation of a reversible equimolar enzyme - antibiotic complex; (b) the irreversible transformation of this complex into a modified enzyme - antibiotic complex; and (c) the breakdown of this latter complex and the concomitant release of a regenerated enzyme and a modified antibiotic molecule. The dissociation constant for step 1 and the rate constants for steps 2 and 3 were measured with various beta-lactam antibiotics. With antibiotic such as benzylpenicillin, which behaves as a good substrate, steps 1 and 2 occur at enzymic velocities, whereas step 3 occurs at a very low velocity and hence is responsible for the low efficiency of the overall process ...
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 ...
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 ...
Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus novo sp. MN-32. The availability of these crystal structures enabled us to model the structure of mammalian CLN2, an enzyme which, when mutated in humans, leads to a fatal neurodegenerative disease. This review compares the structural and enzymatic properties of this newly defined MEROPS family of peptidases, S53, and introduces their new nomenclature ...
en] acyltransferases/*metabolism ; alanine ; carboxypeptidases/*metabolism ; electrophoresis, paper ; glycine ; lysine ; multienzyme complexes/metabolism ; oligopeptides/chemical synthesis ; streptomyces/* ...
D-alanine. Other name(s): D-alanine carboxypeptidase I; DD-carboxypeptidase; D-alanine carboxypeptidase; D-alanyl-D-alanine carboxypeptidase; D-alanine-D-alanine-carboxypeptidase; carboxypeptidase D-alanyl-D-alanine; carboxypeptidase I; UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase; D-alanyl-D-alanine peptidase; DD-peptidase; penicillin binding protein 5; PBP5; PdcA; VanY; VanX (ambiguous). Comments: A bacterial enzyme that requires a divalent cation for activity. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-D-γ-glutamyl-6-carboxy-L-lysyl-D-alanine. Competitively inhibited by penicillins and cephalosporins.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9077-67-2. References:. 1. Izaki, K. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli. J. Biol. Chem. 243 ...
Transgenic technology has become an important technique for crop genetic improvement. The application of well-characterized promoters is essential for developing a vector system for efficient genetic transformation. Therefore, isolation and functional validation of more alternative constitutive promoters to the CaMV35S promoter is highly desirable. In this study, a 2093-bp sequence upstream of the translation initiation codon ATG of AtSCPL30 was isolated as the full-length promoter (PD1). To characterize the AtSCPL30 promoter (PD1) and eight 5′ deleted fragments (PD2-PD9) of different lengths were fused with GUS to produce the promoter::GUS plasmids and were translocated into Nicotiana benthamiana. PD1-PD9 could confer strong and constitutive expression of transgenes in almost all tissues and development stages in Nicotiana benthamiana transgenic plants. Additionally, PD2-PD7 drove transgene expression consistently over twofold higher than the well-used CaMV35S promoter under normal and stress
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
The primary goal of our laboratory is to identify novel pathways that control extracellular matrix(ECM) synthesis and assembly as they relate to fibroproliferative and connective tissue diseases. Our long term goal is to use this knowledge to develop therapeutic strategies for these conditions. Fibroproliferative responses are similar to wound healing processes involving accumulation of contractile myofibroblasts and ECM secretion and assembly. Because organ fibrosis, cardiovascular, metabolic/obesity, and cancer pathologies are now recognized to be impacted by fibroblast-myofibroblast differentiation and ECM remodeling our research is examining novel pathways and control mechanisms in these diseases. Central to our studies is determining the function of Aortic Carboxypeptidase-Like Protein (ACLP), a secreted, collagen-binding protein that enhances fibrosis and myofibroblast differentiation through mechanisms that involve stimulating the transforming growth factor ß (TGFß) receptor signaling ...
May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.
Lysosomal Pro-X Carboxypeptidase/PRCP Overexpression Lysate (Denatured). Tested Reactivity: Hu. Validated: WB. Backed by our 100% Guarantee.
carboxypeptidase M: from human placental microvilli; MW 62kDa; cleaves Arg or Lys from the COOH terminus of synthetic peptides as well as several biologically active substrates; membrane-bound; structurally, catalytically & immunologically distinct from carboxypeptidase A,B,N & H
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
Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
Mouse polyclonal antibody raised against a full-length human AGBL2 protein. AGBL2 (AAH36234, 1 a.a. ~ 902 a.a) full-length human protein. (H00079841-B01P) - Products - Abnova
购买AGBL3兔多克隆抗体(ab107590),AGBL3抗体经WB,IHC-P验证,可与人样本反应。产品出库一年都在质保范围内。中国现货速达。
Complete information for AGBL3 gene (Protein Coding), ATP/GTP Binding Protein Like 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Mouse Monoclonal Anti-Carboxypeptidase A1/CPA1 Antibody (1C12). Validated: WB, Flow, ICC/IF. Tested Reactivity: Human. 100% Guaranteed.
1CBX: Crystal structure of the complex between carboxypeptidase A and the biproduct analog inhibitor L-benzylsuccinate at 2.0 A resolution.
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 ...
Looking for online definition of Carboxypeptidases a in the Medical Dictionary? Carboxypeptidases a explanation free. What is Carboxypeptidases a? Meaning of Carboxypeptidases a medical term. What does Carboxypeptidases a mean?
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)+ ...
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 ...
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. This enzyme catalyses the following chemical reaction Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl--D-alanine This is a zinc enzyme. Catalyses carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Dideberg, O.; Charlier, P.; Dive, G.; Joris, B.; Frère, J.M.; Ghuysen, J.M. (1982). "Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution". Nature. 299 (5882): 469-470. doi:10.1038/299469a0. PMID 7121588. Joris, B.; Van Beeumen, J.; Casagrande, F.; Gerday, C.; Frère, J.-M.; Ghuysen, J.-M. (1983). "The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". Eur. J. Biochem. 130 (1): 53-69. doi:10.1111/j.1432-1033.1983.tb07116.x. ...
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 ...
TY - JOUR. T1 - Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin. AU - Kovács, András. AU - Szabó, László. AU - Longstaff, Colin. AU - Tenekedjiev, Kiril. AU - Machovich, Raymund. AU - Kolev, Krasimir. PY - 2014/1/1. Y1 - 2014/1/1. N2 - 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. 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. Methods and results We used the stable carboxypeptidase B (CPB), which shows the same substrate specificity as TAFIa. If 1.5 - 6 μM fibrinogen was clotted in the presence of 8 ...
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). ...
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 ...
Chronic pain often accompanies immune-related diseases with an elevated level of IgG immune complex (IgG-IC) in the serum and/or the affected tissues though the underlying mechanisms are largely unknown. shown that neuronal FcRI triggers a nonselective cation channel, which may contribute to the IgG-IC-induced excitation of DRG neurons[19,30]. Moreover, TRPC3 acts as a novel and crucial downstream transduction channel mediating… More →. ...
Sphingosine-1-phosphate (S1P) can be an important mediator of inflammation recently shown in studies to increase the excitability of small diameter sensory neurons at least in part via activation of the S1P1 receptor subtype. but not its inactive enantiomer, W140. The hyperalgesic effects of S1P were mimicked by intraplantar injection of the well characterized S1PR1 agonist, SEW2871. The development of S1P-induced hyperalgesia was clogged by apocynin, a NADPH oxidase inhibitor, L-NAME, a non-selective NOS inhibitor and by the potent PN decomposition catalysts (FeTM-4-PyP5+ and MnTE-2-PyP5+). Our findings provide mechanistic insight into the signaling pathways engaged by S1P in the development of hyperalgesia and focus on the contribution of the S1P1 receptor-to-PN signaling in this process. [69; 68] at least in part via INCB8761 activation of S1PR1 [11] and that S1P derived following bioconversion of ceramide, contributes to NGF-induced excitation of rat sensory neurons [70; 36]. Interestingly, ...
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 ...
Looking for online definition of carboxypeptidase in the Medical Dictionary? carboxypeptidase explanation free. What is carboxypeptidase? Meaning of carboxypeptidase medical term. What does carboxypeptidase mean?
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Prostate-specific membrane antigen (PSMA), also known as glutamate carboxypeptidase II (GCPII), is an important diagnostic and therapeutic target in prostate cancer. PSMA/GCPII is also expressed in many healthy tissues, but its function has only been established in the brain and small intestine.
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. The following values were found (the first value applies to the binary complex and the second one to the monomer). The A 1%/280.1 cm values were 19.9 +/- 0.3 and 16.3 +/- 0.3. The partial specific volumes v -0 were 0.707 +/- 0.016 cm3/g and 0.714 +/- 0.015 cm3/g. The sedimentation coefficients S 0/20,w were 4.90 +/- 0.15S and 3.75 +/- 0.15 S. The diffusion coefficients D 0/20,w were (5.8 +/- 0.1) X 10(-7) cm2/s and (6.95 +/- 0.15) X 10(-7) cm2/s. From these data the following values were calculated. Relative molecular masses Mr were 71 000 +/- 4000 and 46 000 +/- 3000. The frictional ratios f/fmin. were 1.37 +/- 0.06 and 1.31 +/- 0.07; assuming a value for the solvation of the molecules (delta = 0.5 g/g) the asymmetry values range from 3 to 5 for the binary complex and from 2 to 4 for the monomer. The Mr values ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Novel human polynucleotide and polypeptide sequences are disclosed that can be used in therapeutic, diagnostic, and pharmacogenomic applications.
Conventional methods for locating the epitope of an antibody on an antigen all require amino acid sequencing at some stage of the protocol. The protein footprinting approach, for example, employs...
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.
The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms The Venus flytrap (Dionaea muscipula) is one of the most well-known carnivorous plants because of its unique ability to capture small animals, usually insects or spiders, through a unique snap-trapping mechanism. The animals are subsequently killed and digested to assimilate nutrients as the plants grow in mineral-deficient soils. We deep sequenced the cDNA from Dionaea traps to obtain transcript libraries, which were used in the mass spectrometry-based identification of the proteins secreted during digestion. The identified proteins consisted of peroxidases, nucleases, phosphatases, phospholipases, a glucanase, chitinases, and proteolytic enzymes, including four cysteine proteases, two aspartic proteases, and a serine carboxypeptidase. The majority of the most abundant proteins were categorized as pathogenesis-related proteins, suggesting that the plants digestive system evolved from ...
The protein composition of the digestive fluid from the Venus flytrap sheds light on prey digestion mechanisms The Venus flytrap (Dionaea muscipula) is one of the most well-known carnivorous plants because of its unique ability to capture small animals, usually insects or spiders, through a unique snap-trapping mechanism. The animals are subsequently killed and digested to assimilate nutrients as the plants grow in mineral-deficient soils. We deep sequenced the cDNA from Dionaea traps to obtain transcript libraries, which were used in the mass spectrometry-based identification of the proteins secreted during digestion. The identified proteins consisted of peroxidases, nucleases, phosphatases, phospholipases, a glucanase, chitinases, and proteolytic enzymes, including four cysteine proteases, two aspartic proteases, and a serine carboxypeptidase. The majority of the most abundant proteins were categorized as pathogenesis-related proteins, suggesting that the plants digestive system evolved from ...
Carboxypeptidase A1 Polyclonal Antibody from Invitrogen for Western Blot and Immunohistochemistry (Paraffin) applications. This antibody reacts with Human samples. Supplied as 100 µg purified antibody (1 mg/ml) in Dulbeccos PBS with 50% glycerol, 150mM NaCl and 0.02% sodium azide; pH 7.4.
CD146, a marker of endothelial cells, promotes tumor progression of many cancers including melanoma and the prostate. Strikingly, several lines of evidence suggest that it is a suppressor of breast cancer (BC) progression. In addition, not only the ligand(s) has not been identified, but CD146-downstream mechanisms remain unknown. Here, we report a novel molecular mechanism by which CD146 acts as a suppressor of breast tumor growth. A novel transcriptional target of CD146-suppressed BC, TimpV, the only endogenous protein inhibitor known for metallocarboxypeptidases, was identified and validated using novel validated Enhanced Green Fluorescent Protein (EGFP)-inducible systems of CD146 expression in both, the weakly and the highly invasive BC cell lines MCF-7 and MDA-MB-231, respectively. CD146/TimpV association was validated by quantitative PCR and immunoblotting experiments in a range of BC cells. In functional experiments, both CD146 induction and siRNA experimental approaches revealed that, ...
Summary of AGBL3 (CCP3, MGC32955) expression in human tissue. Estimation of protein expression could not be performed. View primary data.
Preferential cleavage:
1HYT: Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.
Intradermal injection of granulocyte-macrophage colony-stimulating factor (GM-CSF) in patients with metastatic melanoma recruits dendritic cells. Cytokines, Cellular and Molecular Therapy. 1999 ...
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 ...
Abstract: This study addresses the issues in translating the laboratory derived data obtained during discovery phase of research to a clinical setting using a breast cancer model. Laboratory-based risk assessment indi-cated that a family history of breast cancer, reduced folate carrier 1 (RFC1) G80A, thymidylate synthase (TYMS) 5-UTR 28bp tandem repeat, methylene tetrahydrofolate reductase (MTHFR) C677T and catecholamine-O-methyl transferase (COMT) genetic polymorphisms in one-carbon metabolic pathway increase the risk for breast cancer. Glutamate carboxypeptidase II (GCPII) C1561T and cytosolic serine hydroxymethyl transferase (cSHMT) C1420T polymorphisms were found to decrease breast cancer risk. In order to test the clinical validity of this information in the risk prediction of breast cancer, data was stratified based on number of protective alleles into four categories and in each category sensitivity and 1-specificity values were obtained based on the distribution of number of risk ...
https://doi.org/10.18632/oncotarget.12967 Jae-Hye Lee, Hyun-Soo Cho, Jeong-Ju Lee, Soo Young Jun, Jun-Ho Ahn, Ju-Sik Min, Ji-Yong Yoon, Min-Hyuk Choi, Su-Jin Jeon, Jung Hwa Lim, Cho-Rok Jung, Dae-Soo...
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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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.
A membrane-bound, bacterial enzyme inhibited by penicillin and other β-lactam antibiotics, which acylate the active site serine. Examples are known from peptidase famili
Summary of CPVL () expression in human tissue. Cytoplasmic expression with a granular pattern in macrophages, thyroid glandular cells, cardiac myocytes and renal tubules.
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(Medical Xpress) -- A protein produced by the central nervous system’s support cells seems to play two opposing roles in protecting nerve cells from damage, an animal study by Johns Hopkins researchers suggests: Decreasing ...
Rabbit polyclonal Carboxypeptidase A antibody validated for WB and tested in Human, Mouse, Rat and Pig. Immunogen corresponding to synthetic peptide
did you cpy and paste it to the ticker writing then copied it all together into the signiture ????? I am not to clever in that department ...
Title: Thrombin-Activatable Fibrinolysis Inhibitor. VOLUME: 11 ISSUE: 17. Author(s):Pauline F. Marx. Affiliation:Dept. Vascular Medicine, G1-114, Academic Medical Center, P.O. Box 22660, 1100 DD Amsterdam, The Netherlands.. Keywords:tafi, cpu, cpr, cpb, carboxypeptidase, coagulation, fibrinolysis. Abstract: The coagulation system is a potent mechanism that prevents blood loss after vascular injury. It consists of a number of linked enzymatic reactions resulting in thrombin generation. Thrombin converts soluble fibrinogen into a fibrin clot. The clot is subsequently removed by the fibrinolytic system upon wound healing. Thrombin-activatable fibrinolysis inhibitor (TAFI), which is identical to the previously identified proteins procarboxypeptidase B, R, and U, forms a link between blood coagulation and fibrinolysis. TAFI circulates as an inactive proenzyme in the bloodstream, and becomes activated during blood clotting. The active form, TAFIa, inhibits fibrinolysis by cleaving off C-terminal ...
[38 Pages Report] Check for Discount on 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 Review, H2 2017 report by Global Markets Direct. Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane...
Low blood folate levels result in hyperhomocysteinemia, which has been associated with increased risk for cardiovascular disease, neural tube defects and cognitive deficits. Intake of dietary folates is the chief determinant of blood folate levels. Molecular defects in the intestinal absorption of dietary folates that precipitate low blood folate levels and hyperhomocysteinemia have not been investigated previously. Dietary folates are a mixture of polyglutamylated folates which are digested to monoglutamyl folates by the action of folylpoly-gamma-glutamate carboxypeptidase (FGCP), an enzyme that is anchored to the intestinal brush border membrane and is expressed by the glutamate carboxypepidase II (GCPII) gene. We cloned GCPII cDNA from human intestine and identified both a full-length transcript and a 93 bp shorter transcript lacking exon 18, consistent with the presence of a splice variant. In addition, we identified an H475Y polymorphism in GCPII in DNA samples from a healthy Caucasian population
TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI. The four N-linked glycosylation sequons within the activation peptide were all occupied in bovine TAFI, similar to human TAFI, while the sequon located within the enzyme moiety of the bovine protein was non-glycosylated. The enzymatic stability and the kinetic constants of TAFIa differed somewhat between the two proteins, as did the isoelectric point of TAFI, but not TAFIa. Equivalent to human TAFI, bovine TAFI was a substrate for transglutaminases and could be proteolytically cleaved by trypsin or thrombin/solulin
Various abnormalities of coagulation-fibrinolytic system have been reported in patients with thyroid dysfunction. Several studies indicate that coagulation and fibrinolytic system is disturbed in the patients with hyperthyroidism. The levels of plasm
Using human cancer cells, tumour and blood samples from cancer patients, researchers at Johns Hopkins Medicine have uncovered the role of a neurotransmitter in the spread of aggressive cancers.. Neurotransmitters are chemical "messengers" that transmit impulses from neurons to other target cells.. The work, described in the journal Cell Reports, found that this neurotransmitter, called N-acetyl-aspartyl-glutamate (NAAG) NAAG is more abundant in cancers with a tendency to grow and spread rapidly - or so-called higher grade cancers - than in lower grade tumours, making it a potential marker for tumour progression or regression during cancer therapy, the researchers say.. The experiments also demonstrated that NAAG is a source of glutamate, a chemical that cancer cells use as building blocks to survive, in tumours that express an enzyme called glutamate carboxypeptidase II (GCPII).. The group also discovered that stopping the GCPII from being active by using a drug called 2-PMPA to treat human ...
The intestinal absorption of folate occurs at the monoglutamyl level, and an important measure of food folate bioavailability is how much folate from the food reaches the intestinal sites in forms that can readily be absorbed. In the absence of prote
Perform reliable qPCR with Bio-Rads pre-validated Cpvl primer pair, for the Mouse genome. Designed for SYBR Green-based detection.
We compare recent quantum mechanical computations of alternative reaction pathways for carboxypeptidase A, a zinc proteinase, in an "enzyme environment" to similar calculations in the "gas phase" that include the minimal chemical entities that are required for a non-catalytic reaction. The main question that we address is whether anything may be learned from such reduced representations. Two general acid-general base alternative pathways and one nucleophilic pathway are compared. The original calculations were run on a relatively large model (120 atoms) of the active site of carboxypeptidase A which included zinc and its ligands, as well as the residues Arg145, Arg127, Glu270, a water molecule and a model dipeptide. The "gas-phase" pathways include only the dipeptide, water and Glu270 and serve as models for the non-catalytic pathway. The calculations were performed by semiempirical MNDO/H/d that includes modifications for d-orbital representations as well as for intra- and intermolecular ...
1) De Meester F, et al. (1987) The active sites of the beta-lactamases of Streptomyces cacaoi and Streptomyces albus G.. Biochem J 244(2):427-32 PubMed: 2822004 ...
1) Dehottay P, et al. (1987) Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor.. Eur J Biochem 166(2):345-50 PubMed: 3038538 ...
Page contains details about [email protected] . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com
TY - JOUR. T1 - Identification of Naturally Processed Helper T-Cell Epitopes from Prostate-Specific Membrane Antigen Using Peptide-Based in Vitro Stimulation. AU - Kobayashi, Hiroya. AU - Omiya, Ryusuke. AU - Sodey, Benjamin. AU - Yanai, Mitsuru. AU - Oikawa, Kensuke. AU - Sato, Keisuke. AU - Kimura, Shoji. AU - Senju, Satoru. AU - Nishimura, Yasuharu. AU - Tateno, Masatoshi. AU - Celis, Esteban. PY - 2003/11/1. Y1 - 2003/11/1. N2 - Purpose: There is growing evidence that CD4+ helper T lymphocytes (HTLs) play an essential role in the induction and long-term maintenance of antitumor CTL responses. Thus, approaches to develop effective T-cell-based immunotherapy should focus in the stimulation of both CTLs and HTLs reactive against tumor-associated antigens. The present studies were performed with the purpose of identifying HTL epitopes for prostate-specific membrane antigen (PSMA) for the optimization of vaccines for prostate cancer. Experimental Design: Synthetic peptides from regions of the ...
A 1536-nucleotide-long sequence that carries the ampC beta-lactamase gene of the Escherichia coli K-12 chromosome has been determined. This gene codes for a protein of 377 amino acids, of which the first 19 amino acids form a signal peptide. The molecular weight of the mature enzyme was determined to be 39,600. The ampC beta-lactamase with a substrate specificity for cephalosporins showed no significant sequence homologies with beta-lactamases of the penicillinase type or with D-alanine carboxypeptidases. However, because the region around serine-80 of the ampC beta-lactamase has extensive homology with an active-site fragment of the Pseudomonas aeruginosa cephalosporinase, we suggest that the ampC cephalosporinase as well as related cephalosporinases form a distinct group of serine beta-lactamases that have an evolutionary origin different from that of the serine penicillinases and thus constitute a new class of beta-lactamases.. ...
Journal: EJNMMI - European Journal of Nuclear Medicine and Molecular Imaging ArticleTitle: Prostate-specific membrane antigen PET imaging and immunohistochemistry in adenoid cystic carcinoma-a preliminary analysis
Free Online Library: Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma.(Enzymes and Protein Markers) by Clinical Chemistry; Fibrin Lysine
working under the March of Dimes Prematurity Research Grants have identified genetic markers that help predict the risk of premature birth.. Dr. Jerome F. Strauss III, dean of the Virginia Commonwealth Universitys School of Medicine, found that African American babies are three times more likely than babies of European descent to have genetic variation of the SERPINH1 gene which results to the production of less collagen, and therefore weakened fetal membranes which contributes to an increased chance of premature rupture of the membranes and premature birth.. Dr. Xiaobin Wang, from the Childrens Memorial Hospital in Chicago, Illinois, on the other hand, discovered that a genetic variant of the prolylcarboxypeptidase gene is linked to incidence of preeclampsia, a condition that can develop around the 20th week of gestation, characterized by high blood pressure and high levels of protein in the urine. Preeclampsia is a risk factor for premature birth.. It is believed that identifying the factors ...
Experiments in cell lines have suggested that this presenilin mutation may result in a substantial-or even a complete-loss of γ-secretase activity. Apparent reduced cleavage of multiple γ-secretase substrates, including APP and Notch, has been observed, with minimal production of proteolytic products such as Aβ40, Aβ42, and APP C-terminal fragments (APP-CTFs). The mutant presenilin-1 was appropriately trafficked to the cell surface; however, endoproteolysis of the protein was impaired, which may account for the reduced enzyme activity (Heilig et al., 2010). In a mouse model expressing this mutation, overall Aβ levels were also low, but the Aβ42/Aβ40 ratio was increased and the mouse developed amyloid deposits (Xia et al., 2015; Mar 2015 news).. Rather than causing loss of γ-secretase activity, there is evidence that the L435F mutation in PSEN1 may impair the carboxypeptidase-like activity of γ-secretase, altering the enzymes specificity for APP and favoring the production of Aβ43. ...
Lysosomal Storage Disorders are a class of inherited metabolic conditions that result from alterations in the function of lysosomal enzymes. One example is GM1 Gangliosidosis (GM1), a disorder in which the activity of β-galactosidase is deficient resulting in neurodegeneration and early death. The enzyme, β-gal, is a member of the Lysosomal Multienzyme Complex (LMC), which transports proteins to the lysosome and enables various functions. LMC members include β-gal, α-neuraminidase and the Protective Protein Cathepsin A (PPCA). In a unique ovine model of GM1, there is a primary deficiency in the activity of β- galactosidase and a secondary deficiency in α-neuraminidase activity. The cause of the secondary deficiency in α-neuraminidase activity, which is not seen in any other animal model of GM1, is currently unknown. The α-neuraminidase protein is coded for by the NEU1 gene and is, a glycohydrolitic enzyme that is active in the lysosome. The secondary deficiency of α- neuraminidase seen in our
A method is described for estimating plasma renin activity by using renin substrate present in plasma. This method differs from other indirect renin assay methods by (1) incubation in the absence of ions thus establishing conditions for zero order kinetics for the reaction between endogeneous renin and substrate and (2) the use of angiotensinase inhibitors di-sodium ethylenediamine tetraacetic acid (EDTA) and d-isopropylfluorophosphate (DFP). Recoveries of renin added to plasma in levels similar to those occurring in plasma are 85% SD±7%.. The incubation was done at pH 5.5 which was shown to be the optimum for human renin reacting with human substrate.. By incubating human plasma samples with known quantities of human renin, evidence was obtained suggesting that factors other than enzyme or total substrate concentrations affect the velocity of angiotensin formation. This variability of reaction rate may be explained by the existence of an inhibitor or activator in this system or by a variation ...
Affiliation:神戸大学,医学部附属病院,講師, Research Field:Dermatology,Dermatology,Laboratory medicine,Radiation science, Keywords:Squamous cell carcinoma,炎症反応,CARBOXYPEPTIDASE B,表皮細胞,シクロオキスゲナーゼ2,RADIO-SENCITIZATION,RNAi,紫外線,Flavonoid,BETA-AMYLOID, # of Research Projects:4, # of Research Products:17
Complete information for CPA6 gene (Protein Coding), Carboxypeptidase A6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
BPC-157 2mg/5mg Healing Peptides BPC-157 is a long peptide have 15 amino acids, it is derived from a protective protein found in the stomach. It is a signalling peptide; it signals for certain processes to take place in the body. BPC-157 protects...
References for Abcams Recombinant human UCH37 protein (ab108375). Please let us know if you have used this product in your publication
PSMA兔多克隆抗体(ab41034)可与人样本反应并经WB, ICC/IF实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
Prostate-specific Membrane Antigen Antibody-Drug Conjugate (PSMA ADC) 1301EXT is an open-label, nonrandomized, phase 1 extension study of PSMA ADC administered IV in subjects with progressive CMPC that has progressed after prior taxane therapy. Subjects who have participated in PSMA ADC 1301 and who, in the opinion of the PI, are likely to benefit from continued treatment with PSMA ADC will be enrolled in PSMA ADC 1301EXT ...
Prostate-specific membrane antigen (PSMA) is a transmembrane glycoprotein that is overexpressed in prostate cancer. Radiolabeled small molecules that bind with high affinity to its active extracellular center have emerged as a potential new diagnostic standard of reference for prostate cancer, resulting in images with extraordinary tumor-to-background contrast.
... : Schematic presentation of PRCP roles in mammals This schematic presentation highlights major cell functions, which are regulated by PRCP following stimulation by hormones, neuromediators, or drugs. It appears that PRCP is highly regulated and the target of pharmaceutical intervention. AT2; angiotensin II type 2 receptor, SHP-1; sarcoma homology region 2 domain-containing phosphatase 1 (also known as tyrosin protein phosphatase type 6), LC3-2; microtubule-associated protein 1 light chain 3 type 2, BK; bradykinin, KLF2; Krueppel-like factor 2, eNOS; endothelial nitric oxide synthase, B2; bradykinin B2 receptor, MasR; Mas 1 oncogene, α-MSH; alpha melanocyte stimulating hormone, IL; interleukin, TNF-α; tumor necrosis factor alpha, IFN-γ; interferon gamma, and ICAM-1; intracellular Adhesion molecule 1 ...
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
Anti-Human TAFI Clone 1 - Detects Human Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and activated TAFI. Mouse monoclonal of isotype IgG1.
Anti-Human TAFI Clone 3 - Detects Human Thrombin Activatable Fibrinolysis Inhibitor (TAFI) and activated TAFI. Mouse monoclonal of isotype IgG3.
18 Des 2017 - Sewa Apartemen di Santa Eugènia, Spanyol mulai dari Rp271950/malam. Temukan tempat menginap unik dengan tuan rumah setempat di 191 negara. Serasa di rumah di mana saja bersama Airbnb.
Creative-Proteomics offer cas 338-69-2 D-ALANINE (2,3-13C2, 99%). We are specialized in manufacturing Stabel Isotope Labeled Analytical Standard products.
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Galactosialidosis (MIM 256540) is an autosomal recessive lysosomal storage disease caused by a defect of the protective protein/cathepsin A. Increased amounts of urinary sialic acid-rich oligosaccharides are considered to be an essential diagnostic marker of the disease. We here report a patient with atypical clinical features who consistently has excreted normal amounts of sialyloligosaccharides in the urine. The boy started to have attacks of neuropathic pain associated with hyperesthesia around 1(1/2) years of age. From 4 years of age when his vision was first tested, the patient developed progressive visual loss and at the age of 10 years, macular cherry-red spots were found. At this age, he also had a mild learning disability and clinical examination showed mild facial coarsening, increased lumbar lordosis and pyramidal signs in the legs. In conclusion, the clinical and laboratory features of this patient show that galactosialidosis may be considered in patients even in the absence of ...
Galactosialidosis is a condition that affects many areas of the body. The three forms of galactosialidosis are distinguished by the age at which symptoms develop and the pattern of features.. The early infantile form of galactosialidosis is associated with extensive swelling caused by fluid accumulation before birth (hydrops fetalis), a soft out-pouching in the lower abdomen (an inguinal hernia), and an enlarged liver and spleen (hepatosplenomegaly). Additional features of this form include abnormal bone development (dysostosis multiplex) and distinctive facial features that are often described as "coarse." Some infants have an enlarged heart (cardiomegaly); an eye abnormality called a cherry-red spot, which can be identified with an eye examination; and kidney disease that can progress to kidney failure. Infants with this form usually are diagnosed between birth and 3 months; they typically live into late infancy.. The late infantile form of galactosialidosis shares some features with the early ...
Progenics Pharmaceuticals, Inc., of Tarrytown, N.Y. is a biopharmaceutical company focusing on the development and commercialization of innovative therapeutic products to treat the unmet medical needs of patients with debilitating conditions and life-threatening diseases. The Companys principal programs are directed toward symptom management and supportive care and the treatment of HIV infection and cancer. The Company has five product candidates in clinical development and several others in preclinical development. In symptom management and supportive care, the Company is developing methylnaltrexone (MNTX) to treat the constipation associated with opioid-based pain relievers without interfering with pain relief. MNTX is in pivotal phase 3 clinical testing for treatment of opioid-induced constipation in patients with advanced medical illness. MNTX is also being studied for the management of patients with post-operative bowel dysfunction and relief of opioid-induced constipation in patients with ...
The structure of the human C5aR antagonist, C5a-A8, reveals a three-helix bundle conformation similar to that observed for human C5a-desArg, whereas murine C5a and C5a-desArg both form the canonical four-helix bundle. These conformational differences are discussed in light of the differential C5aR activation properties observed for the human and murine complement anaphylatoxins across species. Complement is an ancient part of the innate immune system that plays a pivotal role in protection against invading pathogens and helps to clear apoptotic and necrotic cells. Upon complement activation, a cascade of proteolytic events generates the complement effectors, including the anaphylatoxins C3a and C5a. Signalling through their cognate G-protein coupled receptors, C3aR and C5aR, leads to a wide range of biological events promoting inflammation at the site of complement activation. The function of anaphylatoxins is regulated by circulating carboxypeptidases that remove their C-terminal arginine ...

Carboxypeptidase T - WikipediaCarboxypeptidase T - Wikipedia

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- ...
more infohttps://en.wikipedia.org/wiki/Carboxypeptidase_T

Carboxypeptidase A definition | Drugs.comCarboxypeptidase A definition | Drugs.com

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 ...
more infohttps://www.drugs.com/dict/carboxypeptidase-a.html

Carboxypeptidase B2 (IPR033849) | InterPro | EMBL-EBICarboxypeptidase B2 (IPR033849) | InterPro | EMBL-EBI

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 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR033849

Zinc D-Ala-D-Ala carboxypeptidase - WikipediaZinc D-Ala-D-Ala carboxypeptidase - Wikipedia

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". ...
more infohttps://en.wikipedia.org/wiki/Zinc_D-Ala-D-Ala_carboxypeptidase

Carboxypeptidases | Harvard Catalyst Profiles | Harvard CatalystCarboxypeptidases | Harvard Catalyst Profiles | Harvard Catalyst

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 ...
more infohttps://connects.catalyst.harvard.edu/Profiles/display/Concept/Carboxypeptidases

Carboxypeptidase E, carboxypeptidase domain (IPR034232) | InterPro | EMBL-EBICarboxypeptidase E, carboxypeptidase domain (IPR034232) | InterPro | EMBL-EBI

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 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR034232

Carboxypeptidase - definition of carboxypeptidase by The Free DictionaryCarboxypeptidase - definition of carboxypeptidase by The Free Dictionary

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 ...
more infohttp://www.thefreedictionary.com/carboxypeptidase

Patent US6780640 - Human carboxypeptidases and polynucleotides encoding the same - Google PatentsPatent US6780640 - Human carboxypeptidases and polynucleotides encoding the same - Google Patents

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 ...
more infohttp://www.google.com/patents/US6780640?dq=7,003,515

Carboxypeptidase A1 Antibody
		        
	Carboxypeptidase A1 Antibody

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 ...
more infohttps://www.thermofisher.com/antibody/product/Carboxypeptidase-A1-Antibody-Polyclonal/PA5-39610

Xaa = any amino acid residue
↓ = cleavage site
P6P5P4P3P2P1P1′
XaaXaaXaaXaaXaaXaanot Ser
Preferential cleavage:more infohttps://www.sigmaaldrich.com/life-science/biochemicals/biochemical-products.html?TablePage=16410493

Anti-Carboxypeptidase A antibody (ab63806) | AbcamAnti-Carboxypeptidase A antibody (ab63806) | Abcam

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 ...
more infohttp://www.abcam.com/carboxypeptidase-a-antibody-ab63806.html

Anti-Carboxypeptidase Y antibody (ab34636) ProtocolsAnti-Carboxypeptidase Y antibody (ab34636) Protocols

Abcam provides specific protocols for Anti-Carboxypeptidase Y antibody (ab34636) : Immunoprecipitation protocols, Western blot ...
more infohttp://www.abcam.com/carboxypeptidase-y-antibody-ab34636-protocols.html

carboxypeptidase A4 ELISA Kits | Biocompare.comcarboxypeptidase A4 ELISA Kits | Biocompare.com

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. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2-321370/ELISA_Kit/ELISA_carboxypeptidase_A4

PBP Isolation and DD-Carboxypeptidase Assay | SpringerLinkPBP Isolation and DD-Carboxypeptidase Assay | SpringerLink

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 ...
more infohttps://link.springer.com/protocol/10.1007%2F978-1-4939-9118-1_20

carboxypeptidase H - Semantic Scholarcarboxypeptidase H - Semantic Scholar

carboxypeptidase H. Known as: Enkephalin-Forming Carboxypeptidase, Enkephalin Synthesizing Carboxypeptidase, Carboxypeptidase E ... Carboxypeptidase E mediates palmitate-induced beta-cell ER stress and apoptosis.. *Kristin D. Jeffrey, Emilyn U. Alejandro, +7 ... Carboxypeptidase E Is a Regulated Secretory Pathway Sorting Receptor: Genetic Obliteration Leads to Endocrine Disorders in ... Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity ...
more infohttps://www.semanticscholar.org/topic/carboxypeptidase-H/24905

Rapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting | SpringerLinkRapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting | SpringerLink

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 ...
more infohttps://link.springer.com/protocol/10.1007%2F978-1-60327-259-9_94

carboxypeptidase L
     Summary Report | CureHuntercarboxypeptidase L Summary Report | CureHunter

... and carboxypeptidase L) stabilizes beta-galactosidase and activates neuraminidase by forming with them a high-molecular-weight ... carboxypeptidase L: Cathepsin A (also named protective protein ... Subscribe to New Research on carboxypeptidase L Cathepsin A ( ... 06/01/1992 - "Ring chromosome 20 and possible assignment of the structural gene encoding human carboxypeptidase-L to the distal ... 01/01/1994 - "The deficiency of the lysosomal protective protein/carboxypeptidase L (CARB L) causes the lysosomal storage ...
more infohttp://www.curehunter.com/public/keywordSummaryC055587-carboxypeptidase-L.do

carboxypeptidase M
     Summary Report | CureHuntercarboxypeptidase M Summary Report | CureHunter

... immunologically distinct from carboxypeptidase A,B,N & H ... carboxypeptidase M: from human placental microvilli; MW 62kDa; ... carboxypeptidase M. Subscribe to New Research on carboxypeptidase M from human placental microvilli; MW 62kDa; cleaves Arg or ... 03/01/2013 - "The potential of carboxypeptidase M as a therapeutic target in cancer.". 01/16/2013 - "Carboxypeptidase M in ... CPM protein, human; Cpm protein, mouse; Cpm protein, rat; carboxypeptidase M, human; carboxypeptidase M, mouse; ...
more infohttp://www.curehunter.com/public/keywordSummaryC058479-carboxypeptidase-M.do

Carboxypeptidases | Carboxypeptidases pathway | Carboxypeptidases inhibitorsCarboxypeptidases | Carboxypeptidases pathway | Carboxypeptidases inhibitors

Check Carboxypeptidases pathway , inhibitors reviews and assay information. ... Carboxypeptidases Inhibitors on signaling pathway are available at Adooq Bioscience. ... Carboxypeptidase G2 (CPG2) Inhibitor is a novel Carboxypeptidase G2 (CPG2) Inhibitor, Antitumor agents. Learn More ... Carboxypeptidase G2 (CPG2) Inhibitor Catalog No. A15035. Quick View .category-products .products-list .btn-quickcart { ...
more infohttps://www.adooq.com/carboxypeptidases.html

RCSB PDB - Protein Feature View 









 - Carboxypeptidase A2 - P48052 (CBPA2 HUMAN)RCSB PDB - Protein Feature View - Carboxypeptidase A2 - P48052 (CBPA2 HUMAN)

Similar to that of carboxypeptidase A EC 3.4.17.1, but with a preference for bulkier C-terminal residues. UniProt ...
more infohttp://www.rcsb.org/pdb/protein/P48052

Carboxypeptidase M Antibody (MA5-26858)
                
                
		        
	Carboxypeptidase M Antibody (MA5-26858)

Invitrogen Anti-Carboxypeptidase M Monoclonal (OTI1F8), Catalog # MA5-26858. Tested in Western Blot (WB) and ... Cite Carboxypeptidase M Monoclonal Antibody (OTI1F8). The following antibody was used in this experiment: Carboxypeptidase M ...
more infohttps://www.thermofisher.com/antibody/product/Carboxypeptidase-M-Antibody-clone-OTI1F8-Monoclonal/MA5-26858

Carboxypeptidase - WikipediaCarboxypeptidase - Wikipedia

... 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 ...
more infohttps://en.wikipedia.org/wiki/Carboxypeptidase

WikiGenes - CPB1 - carboxypeptidase B1 (tissue)WikiGenes - CPB1 - carboxypeptidase B1 (tissue)

A 66-kDa glycosylated carboxypeptidase, plasma pro-carboxypeptidase B (pro-plasma CPB), has recently been identified in human ... To investigate the effect of basic carboxypeptidases on fibrinolysis under conditions of constant carboxypeptidase activity, we ... Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone ... Carboxypeptidase E. Fricker, L.D. Annu. Rev. Physiol. (1988) [Pubmed]. *The bifunctional DCOH protein binds to HNF1 ...
more infohttps://www.wikigenes.org/e/gene/e/1360.html

Carboxypeptidase | definition of carboxypeptidase by Medical dictionaryCarboxypeptidase | definition of carboxypeptidase by Medical dictionary

What is carboxypeptidase? Meaning of carboxypeptidase medical term. What does carboxypeptidase mean? ... Looking for online definition of carboxypeptidase in the Medical Dictionary? carboxypeptidase explanation free. ... Related to carboxypeptidase: dipeptidase, Carboxypeptidase B, Carboxypeptidase E, Carboxypeptidase c, carboxypeptidase G2 ... carboxypeptidase A removes aromatic or branched hydrocarbons, while carboxypeptidase B removes positively charged terminal ...
more infohttp://medical-dictionary.thefreedictionary.com/carboxypeptidase

Carboxypeptidase B2/CPB2 Research Products: Novus BiologicalsCarboxypeptidase B2/CPB2 Research Products: Novus Biologicals

Browse our Carboxypeptidase B2/CPB2 product catalog backed by our Guarantee+. ... Carboxypeptidase B2/CPB2 products available through Novus Biologicals. ... PTMs for Carboxypeptidase B2/CPB2. Learn more about PTMs related to Carboxypeptidase B2/CPB2.. Cleavage. Glycosylation. ... Diseases related to Carboxypeptidase B2/CPB2. Discover more about diseases related to Carboxypeptidase B2/CPB2.. Clostridium ...
more infohttps://www.novusbio.com/common-name/carboxypeptidase-b2-cpb2
  • 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)
  • Humans, animals, and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (wikipedia.org)
  • The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. (novusbio.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)
  • Members of subfamily M14B have longer C-termini than those of subfamily M14A [ PMID: 1449602 ], and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble [ PMID: 7674922 ]. (ebi.ac.uk)
  • 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)
  • 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)
  • Metallocarboxypeptidase D is located in the trans Golgi network where it contributes to the biosynthesis of neuropeptides and peptide hormones (such as insulin) along with carboxypeptidase E. In addition to this role, metallocarboxypeptidase D contributes to the processing of proteins, following the action of furin (an endoprotease located in the trans Golgi network). (wikipedia.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)
  • 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)
  • To this end, new methods for the early detection and prognosis of breast cancer, including circulating proteolytic products of carboxypeptidase N, viable circulating tumor cells, and metastasis-related miRNA, are presented in this issue (12-14). (thefreedictionary.com)
  • Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. (ebi.ac.uk)
  • In fruit fly (Drosophila melanogaster), carboxypeptidase D is known as the silver mutation, with defects causing altered wing shape. (wikipedia.org)

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