Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.
A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC 3.4.2.2 and EC 3.4.12.3.
A ZINC-containing exopeptidase primarily found in SECRETORY VESICLES of endocrine and neuroendocrine cells. It catalyzes the cleavage of C-terminal ARGININE or LYSINE residues from polypeptides and is active in processing precursors of PEPTIDE HORMONES and other bioactive peptides.
A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.
A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on GAMMA-AMINOBUTYRIC ACID mediated synaptic transmission.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The rate dynamics in chemical or physical systems.
A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
The process of cleaving a chemical compound by the addition of a molecule of water.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The sum of the weight of all the atoms in a molecule.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A family of gram-positive, saprophytic bacteria occurring in soil and aquatic environments.
A genus of gram-positive bacteria in the family Thermoactinomycetaceae, that can cause FARMER'S LUNG.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
A genus of gram-positive bacteria that forms a branched mycelium. It commonly occurs as a saprophytic form in soil and aquatic environments.
A carboxypeptidase that is specific for proteins that contain two ALANINE residues on their C-terminal. Enzymes in this class play an important role in bacterial CELL WALL biosynthesis.
A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.
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.
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.
Exclusive legal rights or privileges applied to inventions, plants, etc.
A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidase activity on some substrates. (From Enzyme Nomenclature, 1992) EC 3.4.15.1.
A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.
An antineoplastic agent with alkylating properties. It also acts as a mutagen by damaging DNA and is used experimentally for that effect.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.
An enzyme that catalyzes the transfer of methyl groups from S-adenosylmethionine to free carboxyl groups of a protein molecule forming methyl esters. EC 2.1.1.-.
A method for determining points of contact between interacting proteins or binding sites of proteins to nucleic acids. Protein footprinting utilizes a protein cutting reagent or protease. Protein cleavage is inhibited where the proteins, or nucleic acids and protein, contact each other. After completion of the cutting reaction, the remaining peptide fragments are analyzed by electrophoresis.
Methods used for studying the interactions of antibodies with specific regions of protein antigens. Important applications of epitope mapping are found within the area of immunochemistry.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

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)

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 ...
The anorexigenic neuromodulator α-melanocyte-stimulating hormone (α-MSH; referred to here as α-MSH1-13) undergoes extensive posttranslational processing, and its in vivo activity is short lived due to rapid inactivation. The enzymatic control of α-MSH1-13 maturation and inactivation is incompletely understood. Here we have provided insight into α-MSH1-13 inactivation through the generation and analysis of a subcongenic mouse strain with reduced body fat compared with controls. Using positional cloning, we identified a maximum of 6 coding genes, including that encoding prolylcarboxypeptidase (PRCP), in the donor region. Real-time PCR revealed a marked genotype effect on Prcp mRNA expression in brain tissue. Biochemical studies using recombinant PRCP demonstrated that PRCP removes the C-terminal amino acid of α-MSH1-13, producing α-MSH1-12, which is not neuroactive. We found that Prcp was expressed in the hypothalamus in neuronal populations that send efferents to areas where α-MSH1-13 is ...
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
When expressed in HEK293 cells, this mutation altered the specificity of the carboxypeptidase-like γ-cleavage, but spared the endoproteolytic ε-cleavage of APP, resulting in increased secreted Aβ42, and an increased Aβ42/Aβ40 ratio (Ikeuchi et al., 2008; Li et al., 2016). Similar results were obtained in an in vitro assay using purified proteins to test the ability of this mutant to cleave the APP-C99 substrate (Sun et al., 2017). Levels of the N-terminal fragment (NTF) of presenilin-1 was decreased, suggesting impaired endoproteolysis of the protein. NICD levels were decreased, suggesting reduced Notch cleavage by γ-secretase (Ikeuchi et al., 2008).. Moreover, a cryo-electron microscopy study of the atomic structure of γ-secretase bound to an APP fragment indicated that L381 forms part of one of two PSEN1 β-strands induced by APP binding. These strands, together with an APP β-strand, form a hybrid, three-stranded β-sheet that appears to be indispensable for APP cleavage (Zhou et al., ...
This superfamily consists of structural domains from hydrolytic enzymes that have an alpha/beta fold. These include: cholinesterases, carboxypeptidases, hydrolases, lipases. The ESTHER database (ESTerases and alpha/beta-Hydrolase Enzymes and Relatives) gathers and annotates all the published information related to gene and protein sequences of this superfamily. Structures and families can be found at: http://bioweb.ensam.inra.fr/ESTHER/allstructure and http://bioweb.ensam.inra.fr/ESTHER/general?what=overallTable. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best conserved structural features of the fold. These enzymes have diverged from a common ancestor so as to preserve the arrangement of the catalytic residues, not the ...
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
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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)+ ...
TY - JOUR. T1 - Mapping of the active site of glutamate carboxypeptidase II by site-directed mutagenesis. AU - Mlčochová, Petra. AU - Plechanovová, Anna. AU - Bařinka, Cyril. AU - Mahadevan, Daruka. AU - Saldanha, Jose W.. AU - Rulíšek, Lubomír. AU - Konvalinka, Jan. PY - 2007/9. Y1 - 2007/9. N2 - Human glutamate carboxypeptidase II [GCPII (EC 3.4.17.21)] is recognized as a promising pharmacological target for the treatment and imaging of various pathologies, including neurological disorders and prostate cancer. Recently reported crystal structures of GCPII provide structural insight into the organization of the substrate binding cavity and highlight residues implicated in substrate/inhibitor binding in the S1′ site of the enzyme. To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used ...
TY - JOUR. T1 - Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity. AU - Wlodawer, Alexander. AU - Li, Mi. AU - Gustchina, Alla. AU - Tsuruoka, Naoki. AU - Ashida, Masako. AU - Minakata, Hiroyuki. AU - Oyama, Hiroshi. AU - Oda, Kohei. AU - Nishino, Tokuzo. AU - Nakayama, Toru. N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.. PY - 2004/5/14. Y1 - 2004/5/14. N2 - Kumamolisin-As (previously called ScpA) is the first known example of a collagenase from the sedolisin family (MEROPS S53). This enzyme is active at low pH and in elevated temperatures. In this study that used x-ray crystallographic and biochemical methods, we investigated the structural basis of the preference of this enzyme for collagen and the importance of a glutamate residue in the unique catalytic triad (Ser278-Glu 78-Asp82) for enzymatic activity. Crystal structures of the uninhibited enzyme and its complex with a covalently bound inhibitor, ...
TY - JOUR. T1 - The activation pathway of procarboxypeptidase B from porcine pancreas: Participation of the active enzyme in the proteolytic processing. AU - Villegas, Virtudes. AU - Vendrell, Josep. AU - Avilés, Francesc X.. PY - 1995/1/1. Y1 - 1995/1/1. N2 - The activation process of porcine pancreatic procarboxypeptidase B (pro‐CPB) has been studied in detail by a number of complementary methodologies, and a description of the molecular events that lead to the generation of active carboxypeptidase B (CPB) has been deduced. The generated CPB participates in the degradation of its own activation segment by excising C‐terminal residues from fragments produced by tryptic proteolysis. The trimming action of CPB is, however, not essential for the release of a fully functional enzyme, in contrast to what was previously reported for porcine procarboxypeptidase A (pro‐CPA). In the model presented here, the activation process is solely dependent on the first tryptic cleavage, at the limit ...
2-Guanidinoethylmercaptosuccinic Acid - CAS 77482-44-1 - Calbiochem CAS 77482-44-1 Potent inhibitor of a carboxypeptidase B-like processing enzyme referred to as enkephalin convertase (Ki = 8.8 nM). - Find MSDS or SDS, a COA, data sheets and more information.
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 ...
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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 ...
Cathepsin A is a ubiquitously expressed, multifunctional lysosomal protein. In the lysosome, it binds to neuraminidase and β-galactosidase to activate the former and stabilize the latter, functions that led to the term lysosomal protective protein. It also possesses serine carboxypeptidase activity at acidic pH as well as deamidase and esterase activities at neutral pH. Mutations that disrupt its protective functions are known to cause the lysosomal storage disease, galactosialidosis, in humans (summarized by Hiraiwa [1]). However, its enzymatic activity has garnered the most attention in recent years. Although localized to lysosomes intracellularly, cathepsin A can also be secreted. Extracellularly, it is capable of degrading many bioactive peptides that function in the cardiovascular system, including endothelin-1, bradykinin, and angiotensin I. Because the enzymatic activity of cathepsin A can be targeted separately from its protective functions (2), there has been interest for at ...
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, ...
Recombinant Human Glutamate carboxypeptidase 2 Protein. Synthesized in e. coli. Protein Tag: His. Purity: Greater than 90% as determined by SDS-PAGE. From $88
Carboxypeptidase A (CPA) is a pancreatic exopeptidase which hydrolyses the peptide bond adjacent to the C-terminal end in polypeptide chains. Mast cell carboxypeptidase A (MC-CPA), a part of the peptidase M14 family, is a highly conserved metalloprotease localized to the secretory granules, along with trytases and chymases. MC-CPA is stored as an active enzyme in the granule and is released, along with other inflammatory mediators, upon mast cell degranulation. MC-CPA mirrors pancreatic carboxypeptidase A in cleaving COOH-terminal aromatic and aliphatic amino acid residues. The optimum pH of MC-CPA is between neutral and basic, depending upon the substrate. The MC-CPA gene, CPA3, resides on chromosome 3 and contains 11 exons ...
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 c in the Medical Dictionary? Carboxypeptidase c explanation free. What is Carboxypeptidase c? Meaning of Carboxypeptidase c medical term. What does Carboxypeptidase c mean?
hits GO term 2352 zinc ion binding 2217 proteolysis 2214 metallocarboxypeptidase activity 1438 carboxypeptidase activity 953 metabolic process 940 hydrolase activity, acting on ester bonds 885 hydrolase activity 783 metal ion binding 118 arginine catabolic process to glutamate 118 arginine metabolic process 116 succinylglutamate desuccinylase activity 88 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides 85 peptidase activity 60 aspartoacylase activity 55 metallopeptidase activity 33 cell wall macromolecule catabolic process 32 cytoplasm 28 cell adhesion 23 cytosol 22 membrane 22 arginine catabolic process to succinate 20 nucleus 18 cellular_component 17 cellular cell wall organization 16 vacuole 16 tubulin binding 15 extracellular region 13 serine-type carboxypeptidase activity 11 extracellular space 9 protein side chain deglutamylation 9 C-terminal protein deglutamylation 9 plasma membrane 8 protein deglutamylation 8 biological_process 8 transferase ...
Recombinant Rat Carboxypeptidase A protein (Tagged) is an Escherichia coli Full length protein 111 to 419 aa range, | 85% purity and validated in SDS-PAGE.
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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 ...
View and buy high quality 2-MPPA from Tocris Bioscience. Selective glutamate carboxypeptidase II (GCP II) inhibitor; orally bioavailable.
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Novel human polynucleotide and polypeptide sequences are disclosed that can be used in therapeutic, diagnostic, and pharmacogenomic applications.
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Product Pig Cytosolic carboxypeptidase 4(AGBL1) ELISA kit From B-Gene - A competitive ELISA for quantitative measurement of Porcine Cytosolic carboxypeptidase 4(AGBL1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP SOLUTION*1 vial 12. WASH SOLUTION (100 x)*1 vial 13. BALANCE SOLUTION*1 vial 14. INSTRUCTION*1
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.
CP000859.PE590 Location/Qualifiers FT CDS 660321..661238 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Dole_0590 FT /product=peptidase U61 LD-carboxypeptidase A FT /note=PFAM: peptidase U61 LD-carboxypeptidase A; KEGG: FT sth:STH2808 putative muramoyltetrapeptide carboxypeptidase FT /db_xref=EnsemblGenomes-Gn:Dole_0590 FT /db_xref=EnsemblGenomes-Tr:ABW66400 FT /db_xref=GOA:A8ZU88 FT /db_xref=InterPro:IPR003507 FT /db_xref=InterPro:IPR027461 FT /db_xref=InterPro:IPR027478 FT /db_xref=InterPro:IPR029062 FT /db_xref=InterPro:IPR040449 FT /db_xref=InterPro:IPR040921 FT /db_xref=UniProtKB/TrEMBL:A8ZU88 FT /protein_id=ABW66400.1 FT /translation=MDLAPMSKIKPRALAFGDTIGIAAPAGAFDADRLEKGLSVLQAMG FT FLVRLPDGTHASQRYLAGTDEHRAAMFNNLFADPEIKAVACARGGFGALRMAPLLDMDA FT ITRHPKIFLGFSDISVLLSILGRKAGLITFHGPVVTSLADADDATIASLADALTTTEPL FT RIDLAEGMSLVPGTAQGPVAGGNLASLCQMIGTPWQPAFDGCILFLEETSEPAYRVDRM FT LTQMRLAGCLAGVAGVALGRFDRCGHMDVIFEIVREHLPEGVPVLAGFPVGHNGTNRTL FT PLGVWASLDAENRFLEYHEPALAR ...
Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Mol Microbiol. 2010 Jul; 77(2):300-23 ...
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 ...
Reeck, G.R., Walsh, K.A. and Neurath, H. (1971). „Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry. 10: 4690-4698. PMID 5140186 ...
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.
Xaa = any amino acid residue ↓ = cleavage sitePreferential cleavage: P6P5P4P3P2P1↓P1′ XaaXaaXaaXaaXaaXaa↓not Ser
Figure 1. The ROC curve for EBNA1 IgA marker (Δ = 1.04). The optimized threshold value was defined as the value on the ROC curve with the highest specificity that successfully identified at least 80% of incident NPC cases (80% sensitivity) in this high-risk population. The alternative threshold had the highest specificity while identifying at least 90% of incident NPC.. ...
Enzymes: strong secretion of amylases (α-amylase and glucoamylase); some carboxypeptidase; low tyrosinase ...
Carboxypeptidases cleave at the carboxyl end of the protein. While they can catabolize proteins, they are more often used in ... "Carboxypeptidase". www.chemistry.wustl.edu. Retrieved 2019-03-23. Nelson DL, Cox MM, Lehninger AL (2013). Lehninger principles ... These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. ...
Carboxypeptidase, which is a protease that takes off the terminal amino acid group from a protein ...
CPN2: Carboxypeptidase N subunit 2. *CPOX: coproporphyrinogen oxidase (coproporphyria, harderoporphyria). *DPPA2: Developmental ...
Wang T, Parris J, Li L, Morgan JI (2006). "The carboxypeptidase-like substrate-binding site in Nna1 is essential for the rescue ... ATP/GTP binding protein 1 is gene that encodes the protein known as cytosolic carboxypeptidase 1 (CCP1), originally named NNA1 ... CCP1/NNA1 is a zinc carboxypeptidase that contains nuclear localization signals that was initially cloned from regenerating ... with alleles containing a zinc carboxypeptidase domain and an ATP/GTP binding motif, a protein first identified in alpha- ...
MPI Carboxypeptidase N deficiency; 212070; CPN1 Carcinoid tumors, intestinal; 114900; SDHD Cardiac arrhythmia, ankyrin-B- ...
... carboxypeptidase A2 (CPA2), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. ... Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the CPA3 ... and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases". Proceedings of the ... "Entrez Gene: CPA3 carboxypeptidase A3 (mast cell)". Reynolds DS, Gurley DS, Austen KF (January 1992). "Cloning and ...
SCPEP1: encoding enzyme Retinoid-inducible serine carboxypeptidase. *SEBOX: encoding protein SEBOX homeobox ...
Psi-loop motif from Carboxypeptidase A. Psi-loop motif[edit]. The psi-loop (Ψ-loop) motif consists of two antiparallel strands ...
Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene. The "CPVL" gene is expressed ... "Entrez Gene: CPVL carboxypeptidase, vitellogenic-like". Harris J, Schwinn N, Mahoney JA, Lin HH, Shaw M, Howard CJ, da Silva RP ... Although the primary sequence of CPVL bears every hallmarks of a serine carboxypeptidase, the enzymatic function of CPVL has ... The designation of CPVL is a true serine carboxypeptidase. Although the primary sequence displays the expected serine ...
Carboxypeptidase A5 is an enzyme that in humans is encoded by the CPA5 gene. Carboxypeptidases have functions ranging from ... "Entrez Gene: CPA5 carboxypeptidase A5". Human CPA5 genome location and CPA5 gene details page in the UCSC Genome Browser. ... Members of the A/B subfamily of carboxypeptidases, such as CPA5, contain an approximately 90-amino acid pro region that assists ... 2003). "The imprinted region on human chromosome 7q32 extends to the carboxypeptidase A gene cluster: an imprinted candidate ...
Carboxypeptidase A4 is an enzyme that in humans is encoded by the CPA4 gene. This gene is a member of the carboxypeptidase A/B ... "Entrez Gene: CPA4 carboxypeptidase A4". Human CPA3 genome location and CPA3 gene details page in the UCSC Genome Browser. Human ... Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI (Jul 1999). "Carboxypeptidase A3 (CPA3): a novel gene highly induced ... 2005). "Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the ...
... (EC 3.4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is an enzyme. It ... Yaron A (1976). "Dipeptidyl carboxypeptidase from Escherichia coli". Methods in Enzymology. 45: 599-610. doi:10.1016/s0076-6879 ... Conlin CA, Miller CG (1995). "Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium ...
Carboxypeptidase, a hydrolytic enzyme important in digestion. Another complex ion enzyme is catalase, which decomposes the ...
The structure of carboxypeptidase A. VI. Some Results at 2.0-A Resolution, and the Complex with Glycyl-Tyrosine at 2.8-A ... The Structure of Carboxypeptidase A, IV. Prelimitary Results at 2.8 A Resolution, and a Substrate Complex at 6 A Resolution. ... The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with ... "The Structure of Carboxypeptidase A. III. Molecular Structure at 6 A Resolution," J Mol. Biol. 19, 423-441 (1966). Ludwig, M. L ...
Retinoid-inducible serine carboxypeptidase is an enzyme that in humans is encoded by the SCPEP1 gene. GRCh38: Ensembl release ... Chen J, Streb JW, Maltby KM, Kitchen CM, Miano JM (Sep 2001). "Cloning of a novel retinoid-inducible serine carboxypeptidase ... "Entrez Gene: SCPEP1 serine carboxypeptidase 1". Robb GB, Rana TM (2007). "RNA helicase A interacts with RISC in human cells and ...
Carboxypeptidase A (left) was the first protein structure from Lipscomb's group. Carboxypeptidase A is a digestive enzyme, a ... Carboxypeptidase A digests by chopping off certain amino acids one-by-one from one end of a protein. The size of this structure ... "The Structure of Carboxypeptidase A, IV. Prelimitary Results at 2.8 A Resolution, and a Substrate Complex at 6 A Resolution". ... Carboxypeptidase A was a much larger molecule than anything solved previously. Aspartate carbamoyltransferase. (right) was the ...
1968 - Papain 1969 - Carboxypeptidase A is a zinc metalloprotease. Its crystal structure (PDB file 1CPA) showed the first ... Rees DC, Lipscomb WN (1982). "Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A ... Later a small protein inhibitor of carboxypeptidase was solved (PDB file 4CPA) that mechanically stops the catalysis by ... "The structure of carboxypeptidase A, VII. The 2.0-Å resolution studies of the enzyme and of its complex with glycyltyrosine, ...
... procollagen carboxypeptidase; procollagen carboxy-terminal proteinase; procollagen peptidase, BMP-1, EC 3.4.24.19) merupakan ...
"Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation". Science. 358 (6369): 1448-1453. ...
... produces streptomycin II and carboxypeptidase. List of Streptomyces species LPSN bacterio.net ... "Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties". Biochemistry (Moscow). 75 (8): ...
"Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, ... Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene. The protein encoded by this gene is a membrane-bound ... "Entrez Gene: CPM carboxypeptidase M". Human CPM genome location and CPM gene details page in the UCSC Genome Browser. Fujiwara ... Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain ...
Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene. Carboxypeptidase N is a plasma ... 2000). "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not". J. Immunol. 165 (2 ... "Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.". Microbiol. Immunol. 46 (2): 131-4. doi ... "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1". Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets ...
Matthews KW, Mueller-Ortiz SL, Wetsel RA (Jan 2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Molecular ...
"Entrez Gene: CPN2 carboxypeptidase N, polypeptide 2". Human CPN2 genome location and CPN2 gene details page in the UCSC Genome ... Carboxypeptidase N subunit 2 is an enzyme that in humans is encoded by the CPN2 gene. GRCh38: Ensembl release 89: ... Riley DA, Tan F, Miletich DJ, Skidgel RA (Apr 1999). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) ... "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: ...
However, carboxypeptidases do not have something similar to the C-domain. In carboxypeptidase A, the active site is accessible ...
Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". ... carboxypeptidase A6 (CPA6), and angiotensin-converting enzyme (ACE). These enzymes are sometimes referred to as enkephalinases ... the resulting intermediates are further reduced by the enzyme carboxypeptidase E (CPE; previously known as enkephalin ...
Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". ... They include: Aminopeptidase N (APN) Neutral endopeptidase (NEP) Dipeptidyl peptidase 3 (DPP3) Carboxypeptidase A6 (CPA6) ...
The digestive enzyme carboxypeptidase became the second known zinc-containing enzyme in 1955. Zinc is the fourth most common ... Carboxypeptidase cleaves peptide linkages during digestion of proteins. A coordinate covalent bond is formed between the ... Two examples of zinc-containing enzymes are carbonic anhydrase and carboxypeptidase, which are vital to the processes of carbon ...
Carboxypeptidase T (EC 3.4.17.18, CPT) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction ... an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases". Biochemistry ( ... Carboxypeptidase T at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281-288. doi:10.1111/j.1432- ...
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". ...
This article focuses on four human carboxypeptidases (CPs): two metallo-CPs and two serine CPs. The metallo-CPs are members of ... Cellular carboxypeptidases Immunol Rev. 1998 Feb;161:129-41. doi: 10.1111/j.1600-065x.1998.tb01577.x. ... This article focuses on four human carboxypeptidases (CPs): two metallo-CPs and two serine CPs. The metallo-CPs are members of ...
Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, CPU, and thrombin- ... Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for ...
Definition of carboxypeptidase A. Provided by Stedmans medical dictionary and Drugs.com. Includes medical terms and ... carboxypeptidase A. Pronunciation: kar-bok′sē-pep′ti-dās. Definition: A hydrolase that releases C-terminal amino acids, with ...
Antibodies to human carboxypeptidase B and methods of use thereof. US5593674. Apr 27, 1995. Jan 14, 1997. Genentech, Inc.. ... Carboxypeptidases are proteases that hydrolyze the peptide bonds at the carboxy-terminal end of a chain of amino acids and have ... Plasma carboxypeptidase. US5837458. May 20, 1996. Nov 17, 1998. Maxygen, Inc.. Methods and compositions for cellular and ... Regulation of human zinc carboxypeptidase b-like protein. US20080003673 *. Sep 6, 2005. Jan 3, 2008. Alejandro Abuin. Novel ...
Escherichia coli mutants defective in dipeptidyl carboxypeptidase. C E Deutch and R L Soffer ... Two independent mutants of Escherichia coli deficient in dipeptidyl carboxypeptidase activity (Dep-) were isolated after ... mutants may prove useful for delineating the regulation and cellular function of dipeptidyl carboxypeptidases in higher ... a potent inhibitor of mammalian dipeptidyl carboxypeptidase (angiotensin-converting enzyme, peptidyl dipeptidase, EC 3.4.15.1 ...
carboxypeptidase synonyms, carboxypeptidase pronunciation, carboxypeptidase translation, English dictionary definition of ... carboxypeptidase. n. Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the ... Related to carboxypeptidase: dipeptidase, Carboxypeptidase B, Carboxypeptidase E, Carboxypeptidase c, carboxypeptidase G2 car· ... Carboxypeptidase - definition of carboxypeptidase by The Free Dictionary https://www.thefreedictionary.com/carboxypeptidase ...
This entry represents the carboxypeptidase domain found in carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and ... Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family.. J. ... The carboxypeptidase A family can be divided into four subfamilies: M14A (carboxypeptidase A or digestive), M14B ( ... Carboxypeptidase E in the mouse placenta.. Differentiation 74 648-60 2006. Rawlings ND, Barrett AJ. Evolutionary families of ...
... 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 ...
The term carboxypeptidase P may refer to: Lysosomal Pro-X carboxypeptidase Membrane Pro-X carboxypeptidase This set index page ...
Low P.S., Yuan J. (1996) Rapid Epitope Mapping by Carboxypeptidase Digestion and Immunoblotting. In: Walker J.M. (eds) The ... Hayashi, R., Moore, S., and Stein, W. H. (1973) Carboxypeptidase from yeast:Large scale preparation and the application to COOH ...
Preferential cleavage:
Chowdhury C, Nayak TR, Young KD et al (2010) A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute ... Pal S., Ghosh A.S. (2019) PBP Isolation and DD-Carboxypeptidase Assay. In: Biswas I., Rather P. (eds) Acinetobacter baumannii. ... PBPs are also involved in PG remodeling by catalyzing DD-carboxypeptidase (DD-CPase) and endopeptidase reactions. Though the ... Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli. Trends ...
Similar to that of carboxypeptidase A EC 3.4.17.1, but with a preference for bulkier C-terminal residues. UniProt ...
Plasma carboxypeptidase B (CPB), which is activated by the thrombin/thrombomodulin complex, plays a procoagulant role during ...
Loss of prolyl carboxypeptidase in two-kidney, one-clip goldblatt hypertensive mice. PLoS One. 2015; 10(2):e0117899. ... "Carboxypeptidases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... A D, D-carboxypeptidase is required for Vibrio cholerae halotolerance. Environ Microbiol. 2015 Feb; 17(2):527-40. ... Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. Mol Biol Cell. 2014 ...
Lysosomal protective protein, EC 3.4.16.5 (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin ... CarboxypeptidaseUniRule annotation. ,p>Information which has been generated by the UniProtKB automatic annotation system, ... tr,U3KQU6,U3KQU6_HUMAN Carboxypeptidase OS=Homo sapiens OX=9606 GN=CTSA PE=1 SV=1 ...
Compare carboxypeptidase A4 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, ... carboxypeptidase A4 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool for ... Your search returned 53 carboxypeptidase A4 ELISA ELISA Kit across 8 suppliers. ...
Rabbit polyclonal Carboxypeptidase A antibody validated for WB and tested in Human, Mouse, Rat and Pig. Immunogen corresponding ... All lanes : Anti-Carboxypeptidase A antibody (ab63806) at 4 µg/ml. Lane 1 : Jurkat cell lysate. Lane 2 : Jurkat cell lysate. ... Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys ...
Compare carboxypeptidase, vitellogenic like ELISA Kits from leading suppliers on Biocompare. View specifications, prices, ... carboxypeptidase, vitellogenic like ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a widely used application for ... Your search returned 24 carboxypeptidase, vitellogenic like ELISA ELISA Kit across 3 suppliers. ...
Anti-Carboxypeptidase Y antibody conjugated to Biotin validated for WB, ELISA, IM, Dot. Immunogen corresponding to full length ... This antibody has been assayed against 1.0µg of Carboxypeptidase Y in a standard capture ELISA using Peroxidase conjugated ...
Human glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) is an established marker for prostate-cancer diagnosis as well as a ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II.. Barinka C1, Starkova J, Konvalinka J, ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst ... A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr Sect F Struct Biol Cryst ...
Potent inhibitor of pancreatic carboxypeptidase A with a Ki of 27 nM, and of the serine proteases trypsin, chymotrypsin and ...
Downloading a figure as powerpoint requires a browser with javascript support. Enable javascript and try again For help please contact [email protected] ...
Browse our Carboxypeptidase M Lysate catalog backed by our Guarantee+. ... We offer Carboxypeptidase M Lysates for use in common research applications: Western Blot. Each Carboxypeptidase M Lysate is ... Our Carboxypeptidase M Lysates can be used in a variety of model species: Human. Use the list below to choose the ... Carboxypeptidase M lysate, CPM lysate, EC 3.4.17 lysate, EC 3.4.17.12 lysate ...
Browse our Carboxypeptidase M Protein catalog backed by our Guarantee+. ... Carboxypeptidase M Proteins. We offer Carboxypeptidase M Peptides and Carboxypeptidase M Proteins for use in common research ... Our Carboxypeptidase M Peptides and Carboxypeptidase M Proteins can be used in a variety of model species: Human. Use the list ... Each Carboxypeptidase M Peptide and Carboxypeptidase M Protein is fully covered by our Guarantee+, to give you complete peace ...
Cytosolic carboxypeptidase 4 (EC:3.4.17.-*Search proteins in UniProtKB for this EC number. ... sp,Q96MI9,CBPC4_HUMAN Cytosolic carboxypeptidase 4 OS=Homo sapiens OX=9606 GN=AGBL1 PE=1 SV=3 ...
Carboxypeptidase 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 ...
NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway.. Carrel D1, Du Y, ... NOS1AP Regulates Dendrite Patterning of Hippocampal Neurons through a Carboxypeptidase E-Mediated Pathway ... NOS1AP Regulates Dendrite Patterning of Hippocampal Neurons through a Carboxypeptidase E-Mediated Pathway ... NOS1AP Regulates Dendrite Patterning of Hippocampal Neurons through a Carboxypeptidase E-Mediated Pathway ...
  • In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin. (wikipedia.org)
  • The term carboxypeptidase P may refer to: Lysosomal Pro-X carboxypeptidase Membrane Pro-X carboxypeptidase This set index page lists enzyme articles associated with the same name. (wikipedia.org)
  • Carboxypeptidase T ( EC 3.4.17.18 , CPT ) is an enzyme . (wikipedia.org)
  • Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme. (wikipedia.org)
  • Enzyme activity was highly sensitive to inhibition by 1-(D-3-mercapto-2-methylpropanoyl)-L-proline (SQ 14225), a potent inhibitor of mammalian dipeptidyl carboxypeptidase (angiotensin-converting enzyme, peptidyl dipeptidase, EC 3.4.15.1). (pnas.org)
  • The "go or grow" poten-tial of gliomas is linked to the neuropeptide processing enzyme carboxypeptidase E and mediated by metabolic stress. (thefreedictionary.com)
  • With a New York University Cancer Institute colleague, the researchers reported that the mixture of free-floating blood proteins created by the enzyme carboxypeptidase N accurately predicted the presence of early-stage breast cancer tissue in mice and in a small population of human patients. (thefreedictionary.com)
  • Researchers from the Houston Methodist Research Institute and New York University Cancer Institute, conducted experiments on mice models and breast cancer patients, and found that a mixture of free-floating blood proteins created by carboxypeptidase N or CPN (an enzyme that plays a major role in modifying proteins after they are being created), accurately signalled the early stages of the deadly disease. (thefreedictionary.com)
  • PCR detection of the insertion/ deletion polymorphism of the human angiotensin converting enzyme gene (DCP1) (dipeptidyl carboxypeptidase 1). (thefreedictionary.com)
  • Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. (ebi.ac.uk)
  • Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity. (ebi.ac.uk)
  • A high-resolution carboxypeptidase-Zn 2+ -citrate complex was studied by X-ray diffraction and enzyme kinetics for the first time. (hindawi.com)
  • The citrate molecule acts as a competitive inhibitor of this benchmark zinc-dependent peptidase, chelating the catalytic zinc ion in the active site of the enzyme and inducing a conformational change such that carboxypeptidase adopts the conformation expected to occur by substrate binding. (hindawi.com)
  • Production of MTX from MTX-Phe, catalyzed by bovine pancreas carboxypeptidase A (CPA), was 250-fold faster than the corresponding reaction involving methotrexate-α-alanine, previously the best MTX peptide substrate for the enzyme. (aacrjournals.org)
  • A carboxypeptidase B-like enzyme was detected in the soluble fraction of purified insulin secretory granules, and implicated in insulin biosynthesis. (portlandpress.com)
  • Reduced expression of carboxypeptidase E (CPE), a neuropeptide-processing enzyme, in a cell death-resistant glioma cell line and lower CPE expression levels in the cohort of GBM samples of The Cancer Genome Atlas compared to normal brain control specimens prompted us to analyze the function of CPE as a putative tumor suppressor gene. (biomedsearch.com)
  • The D-alanyl-d-alanine carboxypeptidase enzyme is essential for virulence in the Schu S4 strain of Francisella tularensis and a dacD mutant is able to provide protection against a pneumonic challenge. (bioportfolio.com)
  • The enzyme L,D-carboxypeptidase A is involved in the recycling of bacterial peptidoglycan and is essential in Escherichia coli during stationary phase. (synbiosis.com)
  • Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. (creative-enzymes.com)
  • Glutamate carboxypeptidase II (GCPII) is an enzyme encoded by the FOLH1 (folate hydrolase 1) gene. (reportsnreports.com)
  • There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. (polstate.com)
  • Most scientists in the field now refer to this enzyme as CPA1 , and to a related pancreatic carboxypeptidase as CPA2 . (chemeurope.com)
  • The NH2-terminal amino acid sequence was determined and turned out to be identical to the NH2-terminal sequence of the membrane-bound carboxypeptidase M. By precipitation with antibodies MAX.1 and MAX.11, membrane preparations of macrophages and placental microvilli were almost completely depleted of enzyme activity, indicating that the two antibodies indeed recognize carboxypeptidase M. Immunoreactivity of both antibodies correlates with the reported tissue distribution of enzyme activity. (uni-regensburg.de)
  • Carboxypeptidase E is a peptide processing enzyme, involved in cleaving numerous peptide precursors, including neuropeptides and hormones involved in appetite control and glucose metabolism. (ox.ac.uk)
  • Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules 1 . (elsevier.com)
  • Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (wikipedia.org)
  • Jager M, Lee MJ, Li C, Farmer SR, Fried SK, Layne MD. Aortic carboxypeptidase-like protein enhances adipose tissue stromal progenitor differentiation into myofibroblasts and is upregulated in fibrotic white adipose tissue. (harvard.edu)
  • We offer Carboxypeptidase M Peptides and Carboxypeptidase M Proteins for use in common research applications: Blocking/Neutralizing, Control, ELISA, Protein Array, Western Blot. (novusbio.com)
  • Each Carboxypeptidase M Peptide and Carboxypeptidase M Protein is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • The protein encoded by CPA6 belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino acid, and have functions ranging from digestion of food to selective biosynthesis of neuroendocrine peptides. (antikoerper-online.de)
  • We show here that the Caenorhabditis elegans egl-21 gene encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the nervous system. (jneurosci.org)
  • The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. (genetex.com)
  • PGCP was co-purified from human placenta with lysosomal carboxypeptidase, cathepsin A, lysosomal endopeptidase, cathepsin D, and a gamma-interferon-inducible protein, IP-30, using an affinity chromatography on a Phe-Leu-agarose column. (sigmaaldrich.com)
  • Recombinant Rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids. (biovendor.com)
  • Analysis of the purified carboxypeptidase by SDS/polyacrylamide-gel electrophoresis under either reducing or non-reducing conditions showed it to be a monomeric protein of apparent Mr 55,000. (portlandpress.com)
  • In this study, the regulation of aortic carboxypeptidase-like protein (ACLP) expression in VSMCs was investigated. (ahajournals.org)
  • Carboxypeptidase B (EC 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase B (PCPB), tissue carboxypeptidase B, peptidyl-L-lysine (L-arginine) hydrolaseis a highly pancreas-specific protein (PASP), and has been identified previously as a serum marker for acute pancreatitis and pancreatic graft rejection. (creative-enzymes.com)
  • Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. (creativebiomart.net)
  • Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) - Glutamate carboxypeptidase II (GCPII) is a membrane-bound binuclear zinc metallopeptidase with the highly expressed in nervous and prostatic tissue. (reportsnreports.com)
  • Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) pipeline Target constitutes close to 9 molecules. (reportsnreports.com)
  • The latest report Glutamate Carboxypeptidase 2 - Pipeline Review, H2 2017, outlays comprehensive information on the Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type. (reportsnreports.com)
  • It also reviews key players involved in Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) targeted therapeutics development with respective active and dormant or discontinued projects. (reportsnreports.com)
  • Recombinant trypsin,recombinant carboxypeptidase B and recombinant protein A won the Shanghai high-tech achievement transformation project in Sep.2013. (polstate.com)
  • Additionally, the report provides an overview of key players involved in Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21) targeted therapeutics development and features dormant and discontinued projects. (globalmarketsdirect.com)
  • The report analyses the pipeline products from therapy areas Oncology, Central Nervous System and Toxicologyunder development targeting Glutamate Carboxypeptidase 2 (Folate Hydrolase 1 or Prostate Specific Membrane Antigen or PSMA or Pteroylpoly Gamma Glutamate Carboxypeptidase or Cell Growth Inhibiting Gene 27 Protein or FOLH1 or EC 3.4.17.21). (globalmarketsdirect.com)
  • Our laboratory has identified a secreted matrix protein, aortic carboxypeptidase-like protein (ACLP), which is upregulated in idiopathic pulmonary fibrosis. (bu.edu)
  • Recommended name: Cytosolic carboxypeptidase-like protein 5 EC= 3.4.17. (cusabio.com)
  • It contains Human Carboxypeptidase A2 capture antibody, Human Carboxypeptidase A2 detector antibody (HRP) and a highly purified HEK293-expressed recombinant Human Carboxypeptidase A2 protein. (sinobiological.com)
  • Membrane-bound carboxypeptidase (CP) M is an important regulator of the kallikrein- kinin system via its ability to generate des-Arg-kinin agonists of the G-protein coupled kinin B1 receptor (B1R). (grantome.com)
  • Enzymes that use a metal in the active site are called "metallo-carboxypeptidases" (EC number 3.4.17). (wikipedia.org)
  • 14) Furthermore, environmental exposures, concomitant medication regimens, and the activities of other metabolic enzymes (eg, ACE, carboxypeptidase N) are also likely to influence bradykinin degradation and the risk for acute hypotensive transfusion reactions. (thefreedictionary.com)
  • Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. (thermofisher.com)
  • According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). (thermofisher.com)
  • The Arabidopsis ( Arabidopsis thaliana ) genome encodes 51 proteins annotated as serine carboxypeptidase-like (SCPL) enzymes. (plantphysiol.org)
  • Deconjugation by pure carboxypeptidase A and B was also examined, and hydrolysis by these tissue fluids and enzymes was compared with that mediated by a bacterial cholyglycine hydrolase. (eurekamag.com)
  • Studies using pure enzymes showed that bovine carboxypeptidase A hydrolyzed the cholyl conjugates of the neutral L-.alpha. (eurekamag.com)
  • Shanghai Yaxin Biotechnology company was founded in 2008,which is a high-tech enterprise that focuses on researching and producing the recombinant proteins.YaxinBio is the first and only a company on researching and producing the recombinant carboxypeptidase B and recombinant trypsin.Animal original free enzymes are specially used in the human recombinant insulin production,and exporting abroad. (polstate.com)
  • 1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating proteases activities found in extracted enzymes with lower purity level. (polstate.com)
  • Carboxypeptidase B from Creative Enzymes has been used as a reference for assaying carboxypeptidase activity in lysed pituitary granules derived from the anterior and intermediate lobes of rat. (creative-enzymes.com)
  • The zinc carboxypeptidase family is divided into those enzymes with substrate preferences for an aliphatic residues in the P1' position (the CPA group) and those that prefer basic P1' residues (the CPB group). (triplepointbiologics.com)
  • Prostate-Specific Membrane Antigen (PSMA) is a transmembrane glutamate carboxypeptidase expressed on tumor-associated vasculature that positively regulates angiogenesis in a laminin-dependent manner. (thefreedictionary.com)
  • Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. (thefreedictionary.com)
  • A high-resolution structure of ligand-free human glutamate carboxypeptidase II. (nih.gov)
  • 11CMCG: Synthesis, uptake selectivity, and primate PET of a probe for glutamate carboxypeptidase II (NAALADase). (thefreedictionary.com)
  • ZJ 43 is a potent inhibitor of PSM and PSMAL (glutamate carboxypeptidase II and III). (adooq.com)
  • 2-MPPA is a selective glutamate carboxypeptidase II (GCP-II) inhibitor used in the treatment of neurological disorders associated with excessive activation of glutamatergic systems. (adooq.com)
  • Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate carboxypeptidase/prostate-specific membrane antigen. (sigmaaldrich.com)
  • We describe the identification, cDNA cloning, and biochemical characterization of a new human blood plasma glutamate carboxypeptidase (PGCP). (sigmaaldrich.com)
  • PGCP showed significant amino acid sequence homology to several cocatalytic metallopeptidases including a glutamate carboxypeptidase II also known as N-acetyl-aspartyl-alpha-glutamate carboxypeptidase or as prostate-specific membrane antigen and expressed glutamate carboxypeptidase activity. (sigmaaldrich.com)
  • Inhibition of glutamate carboxypeptidase II (GCPII) has been shown to be neuroprotective in multiple preclinical models in which dysregulated glutamatergic transmission is implicated. (elsevier.com)
  • A series of hydroxamic acids has been prepared as potential inhibitors of glutamate carboxypeptidase II (GCP II). (elsevier.com)
  • Here we report a novel mechanism by which secreted plasma glutamate carboxypeptidase(PGCP) negatively involves Wnt/β-catenin signaling by DKK4 regulation in liver cancer metastasis. (oncotarget.com)
  • Glutamate carboxypeptidase II (GCPII) is a membrane-bound binuclear zinc metallopeptidase with the highest expression levels found in the nervous and prostatic tissue. (eurekaselect.com)
  • C. Barinka, C. Rojas, B. Slusher and M. Pomper, " Glutamate Carboxypeptidase II in Diagnosis and Treatment of Neurologic Disorders and Prostate Cancer", Current Medicinal Chemistry (2012) 19: 856. (eurekaselect.com)
  • This antibody has been assayed against 1.0µg of Carboxypeptidase Y in a standard capture ELISA using Peroxidase conjugated streptavidin and ABTS (2,2'-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) as a substrate for 30 minutes at RT. (abcam.com)
  • The following antibody was used in this experiment: Carboxypeptidase A1 Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-39610, RRID AB_2556162. (thermofisher.com)
  • Carboxypeptidase M Polyclonal antibody specifically detects Carboxypeptidase M in Human samples. (fishersci.com)
  • Carboxypeptidase B2/CPB2 Polyclonal antibody specifically detects Carboxypeptidase B2/CPB2 in Human samples. (fishersci.com)
  • Carboxypeptidase B antibody LS-C713312 is an HRP-conjugated rabbit polyclonal antibody to Carboxypeptidase B (CPB) from human, mouse and rat. (lsbio.com)
  • Carboxypeptidase B antibody LS-C503531 is an AP-conjugated rabbit polyclonal antibody to human Carboxypeptidase B (CPB). (lsbio.com)
  • Immunoperoxidase staining of human pancreas with Rabbit anti Bovine carboxypeptidase A1 antibody ( AHP2054 ) and HISTAR detection kit . (bio-rad-antibodies.com)
  • Rabbit anti Bovine Carboxypeptidase A1 antibody used for the evaluation of carboxypepridase and pro-carboxypeptidase in mouse tissue lysates by western blotting. (bio-rad-antibodies.com)
  • Antigens Carboxypeptidase A2_CPA2 antibody storage GENTAUR recommends for long therm storage to freeze at -24 C. For short time storage up to 30 days we suggest fridge storage at 1 to 10 C. Prevent multiple freeze taw cycles of Antigens Carboxypeptidase A2_CPA2. (antibody-antibodies.com)
  • RP1-Carboxypeptidase-A1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A1. (triplepointbiologics.com)
  • The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-A1. (triplepointbiologics.com)
  • CPB2 is activated by trypsin and acts on carboxypeptidase B substrates. (thermofisher.com)
  • Plasma levels of carboxypeptidase U (CPU, CPB2 or TAFIa) are elevated in patients with acute myocardial infarction. (nih.gov)
  • Potent inhibitor of pancreatic carboxypeptidase A with a Ki of 27 nM, and of the serine proteases trypsin, chymotrypsin and pancreatic elastase, with Ki values of 6.9 nM, 1.83 nM and 4 nM, respectively. (rcsb.org)
  • Carboxypeptidase G2 (CPG2) Inhibitor is a novel Carboxypeptidase G2 (CPG2) Inhibitor, Antitumor agents. (adooq.com)
  • 1998). Among the studied inhibitors, only two are specific for MCP, i.e. , the potato carboxypeptidase inhibitor (PCI) and its close homolog found in tomato plants (TCI). (bio-protocol.org)
  • Enhanced Co 2+ activation and inhibitor binding of carboxypeptidase M at low pH. (portlandpress.com)
  • The inhibitor appeared to cause lysis of E. coli during stationary phase, behavior that is similar to a previously described deletion mutant of L,D-carboxypeptidase A (M. F. Templin, A. Ursinus, and J.-V. Holtje, EMBO J. 18:4108-4117, 1999). (synbiosis.com)
  • CPR (identical to carboxypeptidase U [CPU], plasma carboxypeptidase B [plasma CPB]) has also been described as an inhibitor of fibrinolysis, and termed TAFI (thrombin activatable fibrinolysis inhibitor). (biomedcentral.com)
  • Expression of carboxypeptidase M on mRNA level and enzymatic activity markedly increase during in vitro differentiation of monocytes, according to the described increase in MAX.1 and MAX.11 antigen expression. (uni-regensburg.de)
  • Carboxypeptidases are proteases that hydrolyze the peptide bonds at the carboxy-terminal end of a chain of amino acids and have been identified in a wide variety of cell types and animals. (google.com)
  • Activation peptide of carboxypeptidase B and anionic trypsinogen as early predictors of the severity of acute pancreatitis. (thefreedictionary.com)
  • Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. (prospecbio.com)
  • Methotrexate-α-phenylalanine (MTX-Phe), a second-generation prodrug in the MTX α-peptide series designed for activation to MTX by carboxypeptidase-mAb conjugates, was synthesized by reaction of the p -nitrophenyl ester of 4-amino-4-deoxy-10-methylpteroic acid with l -glutamyl-α- l -phenylalanine. (aacrjournals.org)
  • Carboxypeptidase A usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side chains. (chemeurope.com)
  • Two independent mutants of Escherichia coli deficient in dipeptidyl carboxypeptidase activity (Dep-) were isolated after mutagenesis with ethyl methanesulfonate. (pnas.org)
  • Ghosh AS, Chowdhury C, Nelson DE (2008) Physiological functions of D-alanine carboxypeptidases in Escherichia coli . (springer.com)
  • Chowdhury C, Nayak TR, Young KD et al (2010) A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli . (springer.com)
  • The distribution of PBP5, the major D,D-carboxypeptidase in Escherichia coli, was mapped by immunolabelling and by visualization of GFP fusion proteins in wild-type cells and in mutants lacking one or more D,D-carboxypeptidases. (nih.gov)
  • SNP detection of carboxypeptidase E gene and its association with meat quality and carcass traits in Korean cattle. (thefreedictionary.com)
  • This is the first report of a serine carboxypeptidase-like gene induced by gibberellins in reproductive and vegetative developing tissues in dicotyledoneous plants. (deepdyve.com)
  • This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. (nih.gov)
  • The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE. (elsevier.com)
  • YaxinBio is specialized in the research and the production of Animal Origin Free recombinant carboxypeptidase B and recombinant trypsin, which are of high importance for the production of human recombinant insulin. (thefreedictionary.com)
  • Trypsin activates carboxypeptidase A1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111. (triplepointbiologics.com)
  • Other carboxypeptidases that use active site serine residues are called "serine carboxypeptidases" (EC number 3.4.16). (wikipedia.org)
  • Similar to that of carboxypeptidase A EC 3.4.17.1 , but with a preference for bulkier C-terminal residues. (rcsb.org)
  • carboxypeptidase A removes aromatic or branched hydrocarbons, while carboxypeptidase B removes positively charged terminal lysine or arginine amino acid residues. (thefreedictionary.com)
  • Proprotein convertases (PCs) cleave precursors after dibasic residues, and carboxypeptidases remove basic residues from the C terminals. (jneurosci.org)
  • Two critical processing steps are proteolytic cleavage after dibasic residues by proprotein convertases (PCs) and removal of the dibasic residues from the C terminals of the cleaved peptides by carboxypeptidases. (jneurosci.org)
  • Carboxypeptidase-B sequentially cleaves C-terminal K and R residues. (biovendor.com)
  • Carboxypeptidases (CP), carboxypeptidase N (CPN) and carboxypeptidase R (CPR), have been reported as a protease, which can cleave carboxy-terminal arginine or lysine residues from biologically active peptides, such as C3a and C5a, and regulate their activity. (biomedcentral.com)
  • Background Removal of C-terminal lysine residues that are continuously exposed in lysing fibrin is an established anti-fibrinolytic mechanism dependent on the plasma carboxypeptidase TAFIa, which also removes arginines that are exposed at the time of fibrinogen clotting by thrombin. (elsevier.com)
  • Recommend recombinant carboxypeptidase B lyophilized should be stored under 2-8℃ in sealed container. (polstate.com)
  • Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. (polstate.com)
  • In addition to providing information about the specific role of this exopeptidase in E. coli, the Dep- mutants may prove useful for delineating the regulation and cellular function of dipeptidyl carboxypeptidases in higher organisms. (pnas.org)
  • Pro-(carboxypeptidases A) from whole pig pancreas. (biochemj.org)
  • Sedimentation analysis and light-scattering measurements were made with the two forms of pig pancreas pro-(carboxypeptidase A), in order to determine some of their physical properties. (biochemj.org)
  • Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. (triplepointbiologics.com)
  • Regulation of tissue inflammation by thrombin-activatable carboxypeptidase B (or TAFI). (semanticscholar.org)
  • Generated stable deletion mutant of TAFI with full carboxypeptidase activity without activation. (nih.gov)
  • Carboxypeptidase A2 ( CPA2 ) is a secreted pancreatic procarboxy -peptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. (sinobiological.com)
  • Methods and results We used the stable carboxypeptidase B (CPB), which shows the same substrate specificity as TAFIa. (elsevier.com)
  • Vancomycin and ristocetin are shown to inhibit the hydrolysis of sensitive peptides by the Streptomyces albus G D-alanyl-D carboxypeptidase and the mechanism of inhibition is discussed. (ac.be)
  • Objective To evaluate the impact of alterations in fibrin structure mediated by constitutive carboxypeptidase activity on the function of fibrin as a template for tissue plasminogen activator-(tPA) induced plasminogen activation and its susceptibility to digestion by plasmin. (elsevier.com)
  • Sun L, Guo C, Burnett J, Pan J, Yang Z, Ran Y, Sun D. Association between expression of Carboxypeptidase 4 and stem cell markers and their clinical significance in liver cancer development. (jcancer.org)
  • This study aimed to evaluate the expression of carboxypeptidase 4 (CPA4) in hepatitis, liver cirrhosis and liver cancer tissues, and revealed its clinical significance in liver cancer progression. (jcancer.org)
  • Carbonell, Juan 2004-10-17 00:00:00 A cDNA clone encoding a serine carboxypeptidase (PsCP), isolated from young fruits of Pisum sativum L., was used to study the temporal and spatial expression and hormonal regulation of serine carboxypeptidase during reproductive and vegetative development. (deepdyve.com)
  • Cloning and sequence analysis of cDNA for bovine carboxypeptidase E . Nature , 323 (6087), 461-464. (elsevier.com)
  • Fricker LD , Evans CJ, Esch FS, Herbert E. Cloning and sequence analysis of cDNA for bovine carboxypeptidase E . Nature . (elsevier.com)
  • A novel subfamily of mouse cytosolic carboxypeptidases. (ebi.ac.uk)
  • Loss of prolyl carboxypeptidase in two-kidney, one-clip goldblatt hypertensive mice. (harvard.edu)
  • The novel human proteins (NHPs) described for the first time herein share structural similarity with animal proteases, and especially carboxypeptidases. (google.com)
  • The carboxypeptidase A family can be divided into four subfamilies: M14A (carboxypeptidase A or digestive), M14B (carboxypeptidase H or regulatory), M14C (gamma-D-glutamyl-L-diamino acid peptidase I) and M14D (AGTPBP-1/Nna1-like proteins) [ PMID: 7674922 , PMID: 17244818 ]. (ebi.ac.uk)
  • Hayashi, R., Moore, S., and Stein, W. H. (1973) Carboxypeptidase from yeast:Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. (springer.com)
  • Our Carboxypeptidase M Peptides and Carboxypeptidase M Proteins can be used in a variety of model species: Human. (novusbio.com)
  • Choose from our Carboxypeptidase M Peptides and Proteins. (novusbio.com)
  • The fact that two of the least related proteins within this clade are acyltransferases rather than true serine carboxypeptidases suggests that some or all of the remaining members of this group may have similar activities. (plantphysiol.org)
  • We are investigating the interaction of two proteins, carboxypeptidase M and B1 receptor, on the cell surface that results in increased production of regulatory molecules that affect cell and organ function. (grantome.com)
  • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. (semanticscholar.org)
  • Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form 1 , which differ slightly in relative molecular mass (M r ) 5 . (elsevier.com)
  • 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. (elsevier.com)
  • Carboxypeptidases that cleave positively charged amino acids (arginine, lysine) are called carboxypeptidase B (B for basic). (wikipedia.org)
  • Cholyl-L-lysine and cholyl-L-arginine were also cleaved by serum and plasma, which are known to possess carboxypeptidase activity. (eurekamag.com)
  • Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. (creative-enzymes.com)
  • Carboxypeptidase B is competitively inhibited by arginine and lysine. (polstate.com)
  • The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". Eur. (wikipedia.org)
  • Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. (abcam.com)
  • amino acids with similar specificity as observed for the human pancreatic juice, whereas bovine carboxypeptidase B cleaved the basic amino acid conjugates. (eurekamag.com)
  • These experiments indicate that glycine and taurine amidates of cholic acid differ from a number of other conjugates with neutral and basic amino acid in being resistant to hydrolysis by pancreatic and plasma carboxypeptidases. (eurekamag.com)
  • In this classification system, carboxypeptidases that have a stronger preference for those amino acids containing aromatic or branched hydrocarbon chains are called carboxypeptidase A (A for aromatic/aliphatic). (wikipedia.org)
  • Aspartic protease, [beta]-galactosidase, peroxidase and serine carboxypeptidase were detected in three Ephedra species. (thefreedictionary.com)
  • CPA (carboxypeptidase A) is another MC protease, co-localized with chymase in severe atherosclerotic lesions. (portlandpress.com)
  • Carboxypeptidase A4 (CPA4) is an extracellular metallocarboxypeptidase, which was closely associated with aggressiveness. (medsci.org)
  • Your search returned 53 carboxypeptidase A4 ELISA ELISA Kit across 8 suppliers. (biocompare.com)
  • Your search returned 24 carboxypeptidase, vitellogenic like ELISA ELISA Kit across 3 suppliers. (biocompare.com)
  • Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function. (harvard.edu)
  • NOS1AP regulates dendrite patterning of hippocampal neurons through a carboxypeptidase E-mediated pathway. (nih.gov)
  • Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis. (semanticscholar.org)
  • Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. (ebi.ac.uk)
  • Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. (nih.gov)
  • PBPs are also involved in PG remodeling by catalyzing DD-carboxypeptidase (DD-CPase) and endopeptidase reactions. (springer.com)
  • One Unit of carboxypeptidase B activity hydrolyzes one micromole of hippuryl-L-arginine per minute at 25℃, pH 7.65. (polstate.com)

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