Carboxypeptidases a. Medical search

Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.

Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2.

A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.

A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC 3.4.2.2 and EC 3.4.12.3.

A ZINC-containing exopeptidase primarily found in SECRETORY VESICLES of endocrine and neuroendocrine cells. It catalyzes the cleavage of C-terminal ARGININE or LYSINE residues from polypeptides and is active in processing precursors of PEPTIDE HORMONES and other bioactive peptides.

A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.

A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on GAMMA-AMINOBUTYRIC ACID mediated synaptic transmission.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.

The rate dynamics in chemical or physical systems.

A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.

A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.

The process of cleaving a chemical compound by the addition of a molecule of water.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

The sum of the weight of all the atoms in a molecule.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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. ...

https://en.wikipedia.org/wiki/Protein_metabolism

... some carboxypeptidase; low tyrosinase Aesthetics: pleasant fragrance; accumulation of flavoring compounds Color: low production ...

https://en.wikipedia.org/wiki/Aspergillus_oryzae

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- ...

https://en.wikipedia.org/wiki/AGTPBP1_(gene)

MPI Carboxypeptidase N deficiency; 212070; CPN1 Carcinoid tumors, intestinal; 114900; SDHD Cardiac arrhythmia, ankyrin-B- ...

https://en.wikipedia.org/wiki/List_of_OMIM_disorder_codes

... 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 ... Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI (June 1999). "Carboxypeptidase A3 (CPA3): a novel gene highly induced ...

https://en.wikipedia.org/wiki/CPA3

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 ...

https://en.wikipedia.org/wiki/CPVL

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 ...

https://en.wikipedia.org/wiki/CPA5

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 ...

https://en.wikipedia.org/wiki/CPA4_(gene)

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 ...

https://en.wikipedia.org/wiki/Thomas_A._Steitz

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 ...

https://en.wikipedia.org/wiki/SCPEP1

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 ... Carboxypeptidase A was a much larger molecule than anything solved previously. Aspartate carbamoyltransferase. (right) was the ... Leucine aminopeptidase, (left) a little like carboxypeptidase A, chops off certain amino acids one-by-one from one end of a ...

https://en.wikipedia.org/wiki/William_Lipscomb

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, ...

https://en.wikipedia.org/wiki/List_of_biophysically_important_macromolecular_crystal_structures

"Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation". Science. 358 (6369): 1448-1453. ...

https://en.wikipedia.org/wiki/VASH2

... produces streptomycin II and carboxypeptidase. List of Streptomyces species LPSN bacterio.net ATCC ... "Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties". Biochemistry (Moscow). 75 (8): ...

https://en.wikipedia.org/wiki/Streptomyces_bikiniensis

"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 ...

https://en.wikipedia.org/wiki/CPM_(gene)

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 ...

https://en.wikipedia.org/wiki/CPN1

Matthews KW, Mueller-Ortiz SL, Wetsel RA (Jan 2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Molecular ...

https://en.wikipedia.org/wiki/Kininogen_1

"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: ...

https://en.wikipedia.org/wiki/CPN2

However, carboxypeptidases do not have something similar to the C-domain. In carboxypeptidase A, the active site is accessible ...

https://en.wikipedia.org/wiki/Aspartoacylase

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 ...

https://en.wikipedia.org/wiki/Zinc_in_biology

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 ...

https://en.wikipedia.org/wiki/Met-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) ...

https://en.wikipedia.org/wiki/Enkephalinase

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 ...

https://en.wikipedia.org/wiki/Zinc

Probable carboxypeptidase X1 is an enzyme that in humans is encoded by the CPXM1 gene. The protein encoded by this gene is a ... "Entrez Gene: CPXM1 carboxypeptidase X (M14 family), member 1". Human CPXM1 genome location and CPXM1 gene details page in the ... member of the M14 family of zinc carboxypeptidases; however, the protein has no detectable carboxypeptidase activity. The ...

https://en.wikipedia.org/wiki/CPXM1

... the pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been ... "Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem ... Carboxypeptidase D is an enzyme that in humans is encoded by the CPD gene. The metallocarboxypeptidase family of enzymes is ... "Entrez Gene: CPD carboxypeptidase D". Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" ...

https://en.wikipedia.org/wiki/CPD_(gene)

Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene. This gene encodes a member of the ... "Entrez Gene: CPZ carboxypeptidase Z". Human CPZ genome location and CPZ gene details page in the UCSC Genome Browser. Reznik SE ... This enzyme displays carboxypeptidase activity towards substrates with basic C-terminal residues. It is most active at neutral ... Novikova EG, Reznik SE, Varlamov O, Fricker LD (2000). "Carboxypeptidase Z is present in the regulated secretory pathway and ...

https://en.wikipedia.org/wiki/CPZ_(gene)

It has also been found to affect the activity of carboxypeptidase H and phenylmethylsulfonylfluoride-inhibited carboxypeptidase ... Solov'ev VB, Gengin MT, Sollertinskaia TN, Latynova IV, Zhivaeva LV (2012). "[Effect of selank on the main carboxypeptidases in ...

https://en.wikipedia.org/wiki/Selank

There is evidence that the receptor in the closely related duck hepatitis B virus is carboxypeptidase D. The virions bind to ... Tong S, Li J, Wands JR (1999). "Carboxypeptidase D is an avian hepatitis B virus receptor". Journal of Virology. 73 (10): 8696- ...

https://en.wikipedia.org/wiki/Hepatitis_B

The trypsin then activates additional trypsin, chymotrypsin and carboxypeptidase. The enzymatic mechanism is similar to that of ...

https://en.wikipedia.org/wiki/Trypsin

Polyglutamylation Polyglycylation Acetylation Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron ...

https://en.wikipedia.org/wiki/Detyrosination

... an alanine carboxypeptidase bradykinin is broken down among other enzymes by carboxypeptidase N D-Ala carboxypeptidase is a ... Initial studies on carboxypeptidases focused on pancreatic carboxypeptidases A1, A2, and B in the digestion of food. Most ... Carboxypeptidases act by replacing the substrate water with a carbonyl (C=O) group. The carboxypeptidase A hydrolysis reaction ... Carboxypeptidase E Carboxypeptidase A Enzyme category EC number 3.4 Thrombin-activatable fibrinolysis inhibitor aka plasma ...

https://en.wikipedia.org/wiki/Carboxypeptidase

In contrast to yeast serine carboxypeptidase (CPD-Y) and wheat serine carboxypeptidase II (CPDW-II), Kex1p displays a very ... In contrast to yeast serine carboxypeptidase (CPD-Y) and wheat serine carboxypeptidase II (CPDW-II), Kex1p displays a very ... CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE. *PDB DOI: 10.2210/ ... Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae.. Shilton, B.H., Thomas ...

https://www.rcsb.org/structure/1ac5

Glutamate carboxypeptidase II (GCPII), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase ... glutamate carboxypeptidase II. File:Gcp2-naag.svg. Reaction Scheme of NAAG Degradation by GCPII: GCPII + NAAG → GCPII-NAAG ... Glutamate+carboxypeptidase+II at the US National Library of Medicine Medical Subject Headings (MeSH) ... Ghose S, Weickert CS, Colvin SM, Coyle JT, Herman MM, Hyde TM, Kleinman JE (January 2004). "Glutamate carboxypeptidase II gene ...

https://www.wikidoc.org/index.php/Glutamate_carboxypeptidase_II

3.4.17.19: Carboxypeptidase Taq. This is an abbreviated version!. For detailed information about Carboxypeptidase Taq, go to ...

https://brenda-enzymes.org/all_enzymes.php?ecno=3.4.17.19

Fields of Study , biochemistry , biochemical compounds , enzymes , hydrolases , peptidases , carboxypeptidases , cysteine-type ...

https://agclass.nal.usda.gov/vocabularies/nalt/concept?uri=https%3A//lod.nal.usda.gov/nalt/136576

In addition, the enzyme removes two glutamate residues from the C-terminus of beta-tubulin and detyrosinated alpha-tubulin (from which the C-terminal L-tyrosine has been removed by EC 3.4.17.17 ...

https://enzyme.expasy.org/EC/3.4.17.24

Carboxypeptidase A2 releases a C-terminal amino acid but prefers the bulkier amino acids. ... 200200 is selected from a sequence within the central region of Carboxypeptidase A2. For blocking experiments, a 10 to 100 fold ...

https://abbiotec.com/peptides/carboxypeptidase-a2-peptide?language=en

Dua RD, Dixit A. Carboxypeptidases from goat pancreas. Indian Journal of Biochemistry & Biophysics. 1973 Sep; 10(3): 223-4. ...

https://imsear.searo.who.int/handle/123456789/26457

The aim of this study was to evaluate the potential of in vivo molecular imaging of glutamate carboxypeptidase II (GCPII; ... In vivo Molecular Imaging of Glutamate Carboxypeptidase II Expression in Re-endothelialisation after Percutaneous Balloon ... In vivo Molecular Imaging of Glutamate Carboxypeptidase II Expression in Re-endothelialisation after Percutaneous Balloon ...

https://kups.ub.uni-koeln.de/18653/

Takatsu, Y., Fujita, Y., Tsukamoto, T., Slusher, B. S., & Hashimoto, K. (2011). Orally active glutamate carboxypeptidase II ... Takatsu Y, Fujita Y, Tsukamoto T, Slusher BS, Hashimoto K. Orally active glutamate carboxypeptidase II inhibitor 2-MPPA ... N2 - Glutamate carboxypeptidase II (GCP II) is a glial enzyme responsible for the hydrolysis of N-acetylaspartylglutamate (NAAG ... AB - Glutamate carboxypeptidase II (GCP II) is a glial enzyme responsible for the hydrolysis of N-acetylaspartylglutamate (NAAG ...

https://jhu.pure.elsevier.com/en/publications/orally-active-glutamate-carboxypeptidase-ii-inhibitor-2-mppa-atte-4

MCE提供Carboxypeptidase M/CPM蛋白, Mouse (422a.a, HEK293, His)，体外功能蛋白活性验证，出色的批间稳定性， ... Carboxypeptidase M/CPM Protein, Mouse (422a.a, HEK293, His) 相关产品:. * Carboxypeptidase M/CPM Protein, Mouse (406a.a, HEK293, His ... Carboxypeptidase M/CPM 蛋白, Mouse (422a.a, HEK293, His) 目录号: HY-P73494 Data Sheet 产品使用指南 ... Carboxypeptidase M/CPM Protein, Mouse

https://www.medchemexpress.cn/recombinant-proteins/carboxypeptidase-m-protein-mouse-422a-a-hek293-his.html

dipeptidyl carboxypeptidase 1. *dipeptidyl carboxypeptidase I. *EC 3.4.15.1. *ICH. *kininase II ...

https://medlineplus.gov/genetics/gene/ace/

"Muramoylpentapeptide Carboxypeptidase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, ... This graph shows the total number of publications written about "Muramoylpentapeptide Carboxypeptidase" by people in this ... Below are the most recent publications written about "Muramoylpentapeptide Carboxypeptidase" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Muramoylpentapeptide Carboxypeptidase". ...

https://profiles.rush.edu/display/7732

Plasma carboxypeptidases as regulators of the plasminogen system. J Clin Invest. 1995 Nov. 96(5):2534-8. [QxMD MEDLINE Link]. ...

https://www.medscape.com/answers/209179-172664/what-is-included-in-long-term-monitoring-of-factor-xiii-fxiii-deficiency

The fractionated extracts showed significant activity against carboxypeptidase A and trypsin. Inhibition of these important ... The carboxypeptidase A inhibition assays were modified from described methods [62,63]. Carboxypeptidase A from bovine pancreas ... Hass, G.M.; Ager, S.P.; Le Tourneau, D.; Derr-Makus, J.E. Specificity of the carboxypeptidase inhibitor from potatoes. Plant ... APs are the only known cyanobacteria peptide inhibitors of the pancreatic metalloexopeptidase carboxypeptidase A [5,37,39,40]. ...

https://www.mdpi.com/2072-6651/8/4/108

Analysis of the carboxypeptidase D cytoplasmic domain: Implications in intracellular trafficking. Elena Kalinina, Oleg Varlamov ... Analysis of the carboxypeptidase D cytoplasmic domain: Implications in intracellular trafficking. Journal of cellular ... Analysis of the carboxypeptidase D cytoplasmic domain : Implications in intracellular trafficking. / Kalinina, Elena; Varlamov ... Kalinina, E., Varlamov, O., & Fricker, L. D. (2002). Analysis of the carboxypeptidase D cytoplasmic domain: Implications in ...

https://ohsu.pure.elsevier.com/en/publications/analysis-of-the-carboxypeptidase-d-cytoplasmic-domain-implication-2

Plasma carboxypeptidases as regulators of the plasminogen system. J Clin Invest. 1995 Nov. 96(5):2534-8. [QxMD MEDLINE Link]. ...

https://emedicine.medscape.com/article/209179-questions-and-answers

Glutamate carboxypeptidase II (GCPII) is a 94 kD class II membrane bound zinc metalloenzyme which catalyzes the hydrolysis of ... Barinka C, Rojas C, Slusher BS, Pomper M. "Glutamate carboxypeptidase II in diagnosis and treatment of neurologic disorders and ... Johns Hopkins Drug Discovery - Project - Glutamate Carboxypeptidase II. 53 page-template,page-template-full_width,page-template ... "Discovery of Orally Available Prodrugs of the Glutamate Carboxypeptidase II (GCPII) Inhibitor 2-Phosphonomethylpentanedioic ...

https://drugdiscovery.jhu.edu/our-projects/gcp-ii/

Zn-dependent arginine carboxypeptidase-like family domain assignments . Domain assignment details for each protein include ... Zn-dependent arginine carboxypeptidase-like family domain assignments No domain assignments for these genomes.. Add assignments ... View all assignments containing a Zn-dependent arginine carboxypeptidase-like domain in each group of genomes. ...

https://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/cgi-bin/genome.cgi?sf=159340

Sequencing Grade Carboxypeptidase B, For Mass Spectrometry from China, Chinas leading Recombinant Carboxypeptidase B product ... Producing high quality Carboxypeptidase B, Sequencing Grade Carboxypeptidase B, For Mass Spectrometry products. ... market, With strict quality control Recombinant Carboxypeptidase B factories, ... Recombinant Carboxypeptidase B Carboxypeptidase Enzyme, Animal Origin Free, Carboxypeptidase B, Proteomics Grade ...

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C51 family D-Ala-D-Gly carboxypeptidase. Cell wall hydrolase. 85. (24). ...

https://wwwnc.cdc.gov/eid/article/27/3/20-0852-t2

F. Kasikci, C. X. Niamh, T. Yanık, and P. Y. Loh, "Investigation of the cellular mechanisms underlying the carboxypeptidase E ...

https://open.metu.edu.tr/handle/11511/55719

Recombinant Human Carboxypeptidase B2 is produced by our Mammalian expression system and the target gene encoding Phe23-Val423 ...

https://www.bonopusbio.com/product-page/novoprotein-recombinant-human-carboxypeptidase-b2-cpb2-c-6his

Mouse Carboxypeptidase B1 / CPB1 ELISA Pair Set detection - quantification SEK50386 Sino Biological Pack: ... Mouse Carboxypeptidase B1 / CPB1 ELISA Pair Set. Brand. Sino Biological. short description. The Mouse Carboxypeptidase B1 / ... The minimum detectable dose of Mouse Carboxypeptidase B1 / CPB1 was determined to be approximately 12.5 pg/ml. This is defined ... The minimum detectable dose of Mouse Carboxypeptidase B1 / CPB1 was determined to be approximately 12.5 pg/ml. This is defined ...

https://elisa-kits.de/de/mouse-carboxypeptidase-b1-cpb1-elisa-pair-set.html

title = "Substrate specificity of human carboxypeptidase A6",. abstract = "Carboxypeptidase A6 (CPA6) is an extracellular ... Lyons, P. J., & Fricker, L. D. (2010). Substrate specificity of human carboxypeptidase A6. Journal of Biological Chemistry, 285 ... Lyons, Peter J. ; Fricker, Lloyd D. / Substrate specificity of human carboxypeptidase A6. In: Journal of Biological Chemistry. ... Lyons, PJ & Fricker, LD 2010, Substrate specificity of human carboxypeptidase A6, Journal of Biological Chemistry, vol. 285, ...

https://einstein.pure.elsevier.com/en/publications/substrate-specificity-of-human-carboxypeptidase-a6-2

Unprecedented Binding Mode of Hydroxamate-Based Inhibitors of Glutamate Carboxypeptidase II: Structural Characterization and ... Glutamate Carboxypeptidase IIBiological Activity Inhibitionglutamate carboxypeptidase IIbinding modevivo pharmacokinetics ... Inhibition of glutamate carboxypeptidase II (GCPII) is effective in preclinical models of neurological disorders associated ... Unprecedented Binding Mode of Hydroxamate-Based Inhibitors of Glutamate Carboxypeptidase II: Structural Characterization and ...

https://acs.figshare.com/articles/journal_contribution/Unprecedented_Binding_Mode_of_Hydroxamate_Based_Inhibitors_of_Glutamate_Carboxypeptidase_II_Structural_Characterization_and_Biological_Activity/3199222/1

CARBOXYPEPTIDASE T WITH N-SULFAMOYL-L-GLUTAMIC ACID - 6SN6 , canSARS ...

https://corona-1.cansar.icr.ac.uk/structure/6SN6/3d/6SN6_A

CARBOXYPEPTIDASE B WITH SULPHAMOIL ARGININE - 4Z65 , canSAR Black ... CARBOXYPEPTIDASE B WITH SULPHAMOIL ARGININE EXPRESSION SYSTEM(S ...

https://cansarblack.icr.ac.uk/structure/4Z65/3d/4Z65_A

Glutamate Carboxypeptidase II * Lysine Grant support * R01 CA184228/CA/NCI NIH HHS/United States ...

https://pubmed.ncbi.nlm.nih.gov/25896814/?dopt=Abstract

Structure and Function of REP34 Implicates Carboxypeptidase Activity in Francisella tularensis Host Cell Invasion*. *Geoffrey K ...

https://www.jbc.org/issue/S0021-9258

A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. (wikipedia.org)
In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin. (wikipedia.org)
Glutamate carboxypeptidase II ( GCPII ), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase , or prostate-specific membrane antigen ( PSMA ) is an enzyme that in humans is encoded by the FOLH1 ( folate hydrolase 1 ) gene . (wikidoc.org)
Glutamate carboxypeptidase II (GCP II) is a glial enzyme responsible for the hydrolysis of N-acetylaspartylglutamate (NAAG) into glutamate and N-acetylaspartate (NAA). (elsevier.com)
Carboxypeptidase E (CPE) is the carboxypeptidase B-like enzyme associated with the biosynthesis of numerous peptide hormones and neurotransmitters. (elsevier.com)
1,10-Phenanthroline is an inhibitor of metallopeptidases , with one of the first observed instances reported in carboxypeptidase A. [13] Inhibition of the enzyme occurs by removal and chelation of the metal ion required for catalytic activity, leaving an inactive apoenzyme. (wikipedia.org)
We used haploid genetic screens to identify an unannotated protein, microtubule associated tyrosine carboxypeptidase (MATCAP), as a remaining detyrosinating enzyme. (nki.nl)
Potent inhibitor of a carboxypeptidase B-like processing enzyme referred to as enkephalin convertase (K i = 8.8 nM). (emdmillipore.com)
A bradykinin-degrading enzyme, carboxypeptidase B, weakend this vascular reaction. (nii.ac.jp)
C5a contains 74 amino acids and is rapidly metabolised by a serum enzyme, carboxypeptidase B to a 73 amino acid form, C5a des-Arg. (biolegend.com)
Cathepsin A is a multicatalytic enzyme with carboxypeptidase activities. (medchemexpress.com)

Discovery of Orally Available Prodrugs of the Glutamate Carboxypeptidase II (GCPII) Inhibitor 2-Phosphonomethylpentanedioic Acid (2-PMPA). (jhu.edu)
The permeability-enhancing reactio caused by the protease was not affected by anti histaminic reagent, but was greatly augmented by simultaneous infection of a kinin potentiator, carboxypeptidase N inhibitor. (nii.ac.jp)
Carboxypeptidase g5 (cpdg5) is a selective norepinephrine reuptake inhibitor (ssri) therapy, patients develop a list of doctors in 50 viagra anwendung mg your urine. (childbirthsolutions.com)

All of which refer to the same protein glutamate carboxypeptidase II. (wikidoc.org)
tubulin-glutamate carboxypeptidase. (expasy.org)
Glutamate carboxypeptidase II (GCPII) is a 94 kD class II membrane bound zinc metalloenzyme which catalyzes the hydrolysis of the abundant neuropeptide N-acetylaspartylglutamate (NAAG) to glutamate. (jhu.edu)
Barinka C, Rojas C, Slusher BS, Pomper M. "Glutamate carboxypeptidase II in diagnosis and treatment of neurologic disorders and prostate cancer. (jhu.edu)
Inhibition of glutamate carboxypeptidase II (GCPII) is effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. (figshare.com)
Sodium chloride solution has been used as a component of 10× binding buffer for glutamate carboxypeptidase II (NAALADase) assay. (sigmaaldrich.com)
Association of glutamate carboxypeptidase II (GCPII) haplotypes with breast and prostate cancer risk. (cdc.gov)
The protein acts as a glutamate carboxypeptidase on different alternative substrates, including the nutrient folate and the neuropeptide N-acetyl-l-aspartyl-l-glutamate and is expressed in a number of tissues such as prostate, central and peripheral nervous system and kidney. (origene.com)

Trypsin elastase, carboxypeptidase, and chymotrypsin are produced by the pancreas and released into the duodenum where they act on the chyme. (ubooks.pub)
Shanghai Yaxin Biotechnology Co., Ltd. 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 company on researching and producing the recombinant carboxypeptidase B and recombinant trypsin. (frbiz.com)
The products recombinant trypsin, recombinant carboxypeptidase B and recombinant protein A won the Shanghai high-tech achievement transformation project in Sep.2013. (frbiz.com)
Trypsin then binds to chymotrypsinogen and procarboxypeptidase to convert it into the active chymotrypsin and carboxypeptidase. (oregonstate.education)
Trypsin, chymotrypsin, and carboxypeptidase break down large proteins into smaller peptides, a process called proteolysis . (oregonstate.education)

Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (wikipedia.org)
The protein, known as CPE-delta N, is a form of carboxypeptidase E (CPE). (nih.gov)
Carboxypeptidase cleaves protein. (pharmanotes.org)
The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. (innatedb.com)
The active site residues of carboxypeptidases A and B are conserved in this protein. (innatedb.com)

Initial studies on carboxypeptidases focused on pancreatic carboxypeptidases A1, A2, and B in the digestion of food. (wikipedia.org)
The pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. (tumorportal.org)
CPA3 is one of 8-9 members of the A/B subfamily that includes the well-studied pancreatic enzymes carboxypeptidase A1 ( CPA1 ), carboxypeptidase A2 ( CPA2 ), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. (luxist.com)

Disease relevance of alanine Spherical E. coli due to elevated levels of D - alanine carboxypeptidase. (wikigenes.org)

Carboxypeptidases that cleave positively charged amino acids (arginine, lysine) are called carboxypeptidase B (B for basic). (wikipedia.org)
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. (recombinanttrypsin.com)
Carboxypeptidase B is competitively inhibited by arginine and lysine. (recombinanttrypsin.com)

Lung peptidases, including carboxypeptidase, modulate airway reactivity to intravenous bradykinin. (cdc.gov)

Kex1p is a prohormone-processing serine carboxypeptidase found in Saccharomyces cerevisiae. (rcsb.org)

The enzymes carboxypeptidase and bradykininase also help to facilitate this anti-inflammatory process. (encognitive.com)

Muramoylpentapeptide Carboxypeptidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (rush.edu)
This graph shows the total number of publications written about "Muramoylpentapeptide Carboxypeptidase" by people in this website by year, and whether "Muramoylpentapeptide Carboxypeptidase" was a major or minor topic of these publications. (rush.edu)
Below are the most recent publications written about "Muramoylpentapeptide Carboxypeptidase" by people in Profiles. (rush.edu)

ACE2 is a carboxypeptidase that preferentially removes carboxy-terminal hydrophobic or basic amino acids. (foodpolitics.com)
AF291820 - Homo sapiens ACE-related carboxypeptidase ACE2 mRNA, complete cds. (ucsc.edu)

Kinetic parameters were determined using a panel of synthetic carboxypeptidase substrates, indicating a preference of CPA6 for large hydrophobic C-terminal amino acids and only very weak activity toward small amino acids and histidine. (elsevier.com)
Identification of incompletely processed potential carboxypeptidase E substrates from CpEfatCpEfat mice. (forextrading-madeeasy.com)

Edwards MJ, Moskalyk LA, Donelly-Doman M, Vlaskova M, Noriega FG, Walker VK and Jacobs-Lorena M (2000) Characterization of a carboxypeptidase A gene from the mosquito, Aedes aegypti. (muhlenberg.edu)

The carboxypeptidase A hydrolysis reaction has two mechanistic hypotheses, via a nucleophilic water and via an anhydride. (wikipedia.org)

It utilizes a monoclonal antibody specific for Carboxypeptidase B1 / CPB1 coated on a 96-well plate. (elisa-kits.de)
Standards and samples are added to the wells, and any Carboxypeptidase B1 / CPB1 present binds to the immobilized antibody. (elisa-kits.de)

IMSEAR at SEARO: Carboxypeptidases from goat pancreas. (who.int)
Carboxypeptidases from goat pancreas. (who.int)
Dua RD, Dixit A. Carboxypeptidases from goat pancreas. (who.int)

They also regulate biological processes, such as the biosynthesis of neuroendocrine peptides such as insulin requires a carboxypeptidase. (wikipedia.org)

Another classification system for carboxypeptidases refers to their substrate preference. (wikipedia.org)
In this classification system, carboxypeptidases that have a stronger preference for those amino acids containing aromatic or branched hydrocarbon chains are called carboxypeptidase A (A for aromatic/aliphatic). (wikipedia.org)

The Mouse Carboxypeptidase B1 / CPB1 ELISA Pair Set is for the quantitative determination of Mouse Carboxypeptidase B1 / CPB1. (elisa-kits.de)
The wells are again washed and TMB substrate solution is loaded, which produces color in proportion to the amount of Carboxypeptidase B1 / CPB1 present in the sample. (elisa-kits.de)
The minimum detectable dose of Mouse Carboxypeptidase B1 / CPB1 was determined to be approximately 12.5 pg/ml. (elisa-kits.de)

Those that use an active site cysteine are called "cysteine carboxypeptidase" (or "thiol carboxypeptidases")(EC number 3.4.18). (wikipedia.org)

Carboxypeptidase A2 releases a C-terminal amino acid but prefers the bulkier amino acids. (abbiotec.com)

abstract = "Carboxypeptidase A6 (CPA6) is an extracellular matrix-bound metallocarboxypeptidase (CP) that has been implicated in Duane syndrome, a neurodevelopmental disorder in which the lateral rectus extraocular muscle is not properly innervated. (elsevier.com)

Other carboxypeptidases that use active site serine residues are called "serine carboxypeptidases" (EC number 3.4.16). (wikipedia.org)

cytosolic carboxypeptidase 1. (expasy.org)
cytosolic carboxypeptidase 5. (expasy.org)

No. 200200 is selected from a sequence within the central region of Carboxypeptidase A2. (abbiotec.com)
Optimized DNA sequence encoding Mouse Carboxypeptidase A1(LYS17 - TYR417) preprotein including a C-terminal His tag was expressed in HEK293 cells. (reprokine.com)

Carboxypeptidases hydrolyze peptides at the first amide or polypeptide bond on the C-terminal end of the chain. (wikipedia.org)

A Drosophila pattern recognition receptor contains a peptidoglycan docking groove and unusual L,D-carboxypeptidase activity. (sinica.edu.tw)

Results obtained from present study indicate that the permeabilty-en-hancing reaction induced by the protease is caused by the activation of the kallikrein-kinin cascade in the tissue. (nii.ac.jp)

ACE gene: MedlinePlus Genetics (medlineplus.gov)

Toxins | Free Full-Text | Morphologic, Phylogenetic and Chemical Characterization of a Brackish Colonial Picocyanobacterium ... (mdpi.com)

Factor XIII Deficiency Follow-up: Further Outpatient Care, Further Inpatient Care, Inpatient & Outpatient Medications (medscape.com)

Factor XIII Deficiency: Practice Essentials, Background, Pathophysiology (medscape.com)

Factor XIII Deficiency Clinical Presentation: History, Physical, Causes (medscape.com)

Hemophilia B (Factor IX Deficiency): Practice Essentials, Background, Pathophysiology (medscape.com)

Information on EC 2.3.1.283 - 2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase - BRENDA Enzyme Database (brenda-enzymes.org)

Epatite B - Wikipedia (it.wikipedia.org)

Alexa Fluor® 647 anti-human ACE2 Antibody, ACE2, A20069I (biolegend.com)

Preclinical evaluation of FAP-2286 for fibroblast activation protein targeted radionuclide imaging and therapy | SpringerLink (link.springer.com)

SMART: TBC domain annotation (smart.embl-heidelberg.de)

IUCr) Structure determination of human semaphorin 4D as an example of the use of MAD in non-optimal cases (journals.iucr.org)

Three cases of toxic skin eruptions due to methotrexate and a compilation of methotrexate induced skin eruptions (escholarship.org)

PeptiQuant? Plus Custom Proteomics Kits - MRM Proteomics (mrmproteomics.com)

Atsushi Kato - Research Output

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Bacterial protein signals are associated with Crohn's disease | Gut (gut.bmj.com)

Carboxypeptidase(CPG2) | TargetMol (targetmol.com)

Human IgA2(Immunoglobulin A2) ELISA Kit - Enzyme-linked Immunosorbent Assay Kits (kits-elisa.com)

MonarchBase - Protein-coding gene (monarchbase.umassmed.edu)

Enzyme Markers Monoclonal and Polyclonal Antibody Purification (recombinanttrypsin.com)

China Shanghai Yaxin Biotechnology Co.,Ltd. Mapa do Site (portuguese.recombinanttrypsin.com)

Network Portal - Gene BSU40630 (networks.systemsbiology.net)

Totoki, T.<... (kyushu-u.pure.elsevier.com)

PDB 7XOA | Chain SARS-COV-2 OMICRON BA.2 VARIANT SPIKE TRIMER WITH ONE MOUSE ACE2 BOUND | 7XOA_A | 3D Structure | canSARS (corona-1.cansar.icr.ac.uk)

PDB 3FEC | Chain CRYSTAL STRUCTURE OF HUMAN GLUTAMATE CARBOXYPEPTIDASE III (GCPIII/NAALADASE II), PSEUDO-UNLIGANDED | 3FEC_A |... (corona-1.cansar.icr.ac.uk)

China Shanghai Yaxin Biotechnology Co.,Ltd. company profile (recombinanttrypsin.com)

Anatomy1

Organisms1

Chemicals and Drugs14

Analytical, Diagnostic and Therapeutic Techniques and Equipment3

Phenomena and Processes10

Information Science3

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

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

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

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

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

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

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

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

Carboxypeptidases

Carboxypeptidases A

Lysine Carboxypeptidase

Carboxypeptidase B

Carboxypeptidase H

Cathepsin A

Penicillin G

Amino Acid Sequence

Molecular Sequence Data

Substrate Specificity

Peptide Hydrolases

Amino Acids

Endopeptidases

Kinetics

Pancreas

Sequence Homology, Amino Acid

Cloning, Molecular

Chymotrypsin

Trypsin

Hydrolysis

Hydrogen-Ion Concentration

Base Sequence

Binding Sites

Peptide Fragments

Peptides

Sequence Alignment

Molecular Weight

Models, Molecular

Cattle

Protein Conformation

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

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

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

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

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

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

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

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

CPA3/MC-CPA Polyclonal Antibody, ALEXA FLUOR® 488 Conjugated - Bioss

RCSB PDB - 1AYE: HUMAN PROCARBOXYPEPTIDASE A2

Recombinant Rat Carboxypeptidase A protein (Tagged) (ab235686) | Abcam

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Yamaha A-S500 Integrated Amp, Remote, Optional Ipod Dock, Ex Sound, Powerful, Nice features | Solid state | Audiogon

Application of multi-block approach in the immersed boundary-lattice Boltzmann method for viscous fluid flows | Scholar[email protected]

Multi-block regression based on combinations of orthogonalisation, PLS-regression and canonical correlation analysis| Nofima

Sequence-Controlled Multi-Block Glycopolymers to Inhibit DC-SIGN-gp120 Binding - Zhang - 2013 - Angewandte Chemie International...

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