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 are a group of enzymes that catalyze the cleavage of peptide bonds at the carboxyl-terminal end of polypeptides or proteins. They specifically remove the last amino acid residue from the protein chain, provided that it has a free carboxyl group and is not blocked by another chemical group. Carboxypeptidases are classified into two main types based on their catalytic mechanism: serine carboxypeptidases and metallo-carboxypeptidases.

Serine carboxypeptidases, also known as chymotrypsin C or carboxypeptidase C, use a serine residue in their active site to catalyze the hydrolysis of peptide bonds. They are found in various organisms, including animals and bacteria.

Metallo-carboxypeptidases, on the other hand, require a metal ion (usually zinc) for their catalytic activity. They can be further divided into several subtypes based on their structure and substrate specificity. For example, carboxypeptidase A prefers to cleave hydrophobic amino acids from the carboxyl-terminal end of proteins, while carboxypeptidase B specifically removes basic residues (lysine or arginine).

Carboxypeptidases have important roles in various biological processes, such as protein maturation, digestion, and regulation of blood pressure. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

Carboxypeptidases A are a group of enzymes that play a role in the digestion of proteins. They are found in various organisms, including humans, and function to cleave specific amino acids from the carboxyl-terminal end of protein substrates. In humans, Carboxypeptidase A is primarily produced in the pancreas and secreted into the small intestine as an inactive zymogen called procarboxypeptidase A.

Procarboxypeptidase A is activated by trypsin, another proteolytic enzyme, to form Carboxypeptidase A1 and Carboxypeptidase A2. These enzymes have different substrate specificities, with Carboxypeptidase A1 preferentially cleaving aromatic amino acids such as phenylalanine and tyrosine, while Carboxypeptidase A2 cleaves basic amino acids such as arginine and lysine.

Carboxypeptidases A play a crucial role in the final stages of protein digestion by breaking down large peptides into smaller di- and tripeptides, which can then be absorbed by the intestinal epithelium and transported to other parts of the body for use as building blocks or energy sources.

Lysine carboxypeptidase is not a widely recognized or used medical term. However, in biochemistry, carboxypeptidases are enzymes that cleave peptide bonds at the carboxyl-terminal end of a protein or peptide. If there is a specific enzyme named "lysine carboxypeptidase," it would be an enzyme that selectively removes lysine residues from the carboxyl terminus of a protein or peptide.

There are several enzymes that can act as carboxypeptidases, and some of them have specificities for certain amino acids, such as arginine or lysine. These enzymes play important roles in various biological processes, including protein degradation, processing, and regulation.

It's worth noting that the term "lysine carboxypeptidase" may refer to different enzymes depending on the context, such as bacterial or mammalian enzymes, and they may have different properties and functions.

Carboxypeptidase B is a type of enzyme that belongs to the peptidase family. It is also known as carboxypeptidase B1 or CpB. This enzyme plays a crucial role in the digestion of proteins by cleaving specific amino acids from the carboxyl-terminal end of polypeptides.

Carboxypeptidase B preferentially removes basic arginine and lysine residues from protein substrates, making it an essential enzyme in various physiological processes, including blood clotting, hormone processing, and neuropeptide metabolism. It is synthesized as an inactive zymogen, procarboxypeptidase B, which is converted to its active form upon proteolytic activation.

In addition to its physiological functions, carboxypeptidase B has applications in research and industry, such as protein sequencing, peptide synthesis, and food processing.

Carboxypeptidase H is also known as carboxypeptidase E or CPE. It is an enzyme that plays a role in the processing and activation of neuropeptides, which are small protein-like molecules that function as chemical messengers within the nervous system. Carboxypeptidase H/E is responsible for removing certain amino acids from the end of newly synthesized neuropeptides, allowing them to become biologically active. It is widely expressed in the brain and other tissues throughout the body.

Cathepsin A is a lysosomal protein that belongs to the peptidase family. It plays a role in various biological processes, including protein degradation and activation, cell signaling, and inflammation. Cathepsin A has both endopeptidase and exopeptidase activities, which allow it to cleave and process a wide range of substrates.

In addition to its enzymatic functions, cathepsin A also plays a structural role in the formation and stability of the protective protein complex called the "serglycin-cathepsin A proteoglycan complex." This complex protects certain proteases from degradation and helps regulate their activity within the lysosome.

Deficiencies or mutations in cathepsin A have been linked to several diseases, including a rare genetic disorder called galactosialidosis, which is characterized by developmental delays, coarse facial features, and progressive neurological deterioration.

Penicillin G is a type of antibiotic that belongs to the class of medications called penicillins. It is a natural antibiotic derived from the Penicillium fungus and is commonly used to treat a variety of bacterial infections. Penicillin G is active against many gram-positive bacteria, as well as some gram-negative bacteria.

Penicillin G is available in various forms, including an injectable solution and a powder for reconstitution into a solution. It works by interfering with the ability of bacteria to form a cell wall, which ultimately leads to bacterial death. Penicillin G is often used to treat serious infections that cannot be treated with other antibiotics, such as endocarditis (inflammation of the inner lining of the heart), pneumonia, and meningitis (inflammation of the membranes surrounding the brain and spinal cord).

It's important to note that Penicillin G is not commonly used for topical or oral treatment due to its poor absorption in the gastrointestinal tract and instability in acidic environments. Additionally, as with all antibiotics, Penicillin G should be used under the guidance of a healthcare professional to ensure appropriate use and to reduce the risk of antibiotic resistance.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

The pancreas is a glandular organ located in the abdomen, posterior to the stomach. It has both exocrine and endocrine functions. The exocrine portion of the pancreas consists of acinar cells that produce and secrete digestive enzymes into the duodenum via the pancreatic duct. These enzymes help in the breakdown of proteins, carbohydrates, and fats in food.

The endocrine portion of the pancreas consists of clusters of cells called islets of Langerhans, which include alpha, beta, delta, and F cells. These cells produce and secrete hormones directly into the bloodstream, including insulin, glucagon, somatostatin, and pancreatic polypeptide. Insulin and glucagon are critical regulators of blood sugar levels, with insulin promoting glucose uptake and storage in tissues and glucagon stimulating glycogenolysis and gluconeogenesis to raise blood glucose when it is low.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Chymotrypsin is a proteolytic enzyme, specifically a serine protease, that is produced in the pancreas and secreted into the small intestine as an inactive precursor called chymotrypsinogen. Once activated, chymotrypsin helps to digest proteins in food by breaking down specific peptide bonds in protein molecules. Its activity is based on the recognition of large hydrophobic side chains in amino acids like phenylalanine, tryptophan, and tyrosine. Chymotrypsin plays a crucial role in maintaining normal digestion and absorption processes in the human body.

Trypsin is a proteolytic enzyme, specifically a serine protease, that is secreted by the pancreas as an inactive precursor, trypsinogen. Trypsinogen is converted into its active form, trypsin, in the small intestine by enterokinase, which is produced by the intestinal mucosa.

Trypsin plays a crucial role in digestion by cleaving proteins into smaller peptides at specific arginine and lysine residues. This enzyme helps to break down dietary proteins into amino acids, allowing for their absorption and utilization by the body. Additionally, trypsin can activate other zymogenic pancreatic enzymes, such as chymotrypsinogen and procarboxypeptidases, thereby contributing to overall protein digestion.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

... 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 ...
The term carboxypeptidase P may refer to: Lysosomal Pro-X carboxypeptidase Membrane Pro-X carboxypeptidase This set index page ...
... carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme. ... Muramoyltetrapeptide+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Metz R, Henning S, Hammes WP (March 1986). "LD-carboxypeptidase activity in Escherichia coli. II. Isolation, purification and ... DasGupta H, Fan DP (July 1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium ...
... carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine ... Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active ... Song L, Fricker LD (1995). "Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, ... Carboxypeptidase+D at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.16). ...
... (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl ... Glutamate carboxypeptidase II Goldman P, Levy CC (October 1967). "Carboxypeptidase G: purification and properties". Proceedings ... Glutamate+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17) ... Sherwood RF, Melton RG, Alwan SM, Hughes P (May 1985). "Purification and properties of carboxypeptidase G2 from Pseudomonas sp ...
... (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable ... Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, ... and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A ( ... "Entrez Gene: CPB2 carboxypeptidase B2 (plasma)". Bouma BN, Mosnier LO (2005). "Thrombin activatable fibrinolysis inhibitor ( ...
... (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is ... "Entrez Gene: CPE carboxypeptidase E". Fricker LD (1988). "Carboxypeptidase E". Annual Review of Physiology. 50: 309-21. doi: ... Biology portal Carboxypeptidase Carboxypeptidase A GRCh38: Ensembl release 89: ENSG00000109472 - Ensembl, May 2017 GRCm38: ... fills in for carboxypeptidase E in this organism. In humans, CPE is encoded by the CPE gene. Carboxypeptidase E functions in ...
... may refer to: Angiotensin-converting enzyme (ACE) Peptidyl-dipeptidase Dcp This set index page ...
... may refer to: Glutamate carboxypeptidase, an enzyme Gamma-glutamyl hydrolase, an enzyme This set index page ...
... (EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L- ... Plasma carboxypeptidase B (carboxypeptidase B2) is responsible for converting the C5a protein into C5a des-Arg, with one less ... Folk JE (1970). "Carboxypeptidase B (porcine pancreas)". Methods Enzymol. 19: 504-508. doi:10.1016/0076-6879(70)19036-7. ... The MEROPS online database for peptidases and their inhibitors: M14.003 Carboxypeptidase+B at the U.S. National Library of ...
D-alanine carboxypeptidase I, DD-carboxypeptidase, D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanine-D ... carboxypeptidase, carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine ... Muramoylpentapeptide+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Purification and properties of two D-alanine carboxypeptidases from Escherichia coli". The Journal of Biological Chemistry. 243 ...
... (EC 3.4.17.20, arginine carboxypeptidase, carboxypeptidase R, plasma carboxypeptidase B, thrombin- ... Wang W, Hendriks DF, Scharpé SS (June 1994). "Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen ... plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U. Carboxypeptidase Eaton DL, ... Carboxypeptidase+U at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ...
... (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ... Carboxypeptidase+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.16). ... Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... deamidase, lysosomal carboxypeptidase A, phaseolin) is an enzyme. This enzyme catalyses the following chemical reaction Release ...
... inhibitor Carboxypeptidase B Carboxypeptidase Carboxypeptidase E Christianson DW, Lipscomb WN (February 1989 ... This property of carboxypeptidase A led to the first clause of Daniel E. Koshland, Jr.'s "induced fit" hypothesis. The S1 sub- ... Carboxypeptidase A (CPA) contains a zinc (Zn2+) metal center in a tetrahedral geometry with amino acid residues in close ... Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with ...
... is also known as: carboxypeptidase N arginine carboxypeptidase kininase I anaphylatoxin inactivator ... Lysine carboxypeptidase is in sub-subclass 17: metallocarboxypeptidases. This subclass first defines lysine carboxypeptidase as ... Lysine carboxypeptidase's EC number is 3.4.17.3. The first number in an EC number indicates the main class that the enzyme ... Lysine carboxypeptidase (EC 3.4.17.3) is an enzyme. This enzyme catalyses the following chemical reaction: Release of a C- ...
Carboxypeptidase A inhibitor Carboxypeptidase GRCh38: Ensembl release 89: ENSG00000165078 - Ensembl, May 2017 GRCm38: Ensembl ... Carboxypeptidase A6 (CPA6) is a metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene. It is highly ... "Entrez Gene: Carboxypeptidase A6". Retrieved 2011-11-25. Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of ... The protein encoded by this gene belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino ...
... may refer to: Lysine carboxypeptidase, an enzyme Carboxypeptidase U, an enzyme This set index page ...
Carboxypeptidase+M at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... Carboxypeptidase M (EC 3.4.17.12, CPM) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of C- ... Deddish PA, Skidgel RA, Erdös EG (July 1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. ... Similarity to carboxypeptidase H (enkephalin convertase)". The Biochemical Journal. 261 (1): 289-91. PMC 1138816. PMID 2775217 ...
... may refer to: Muramoylpentapeptide carboxypeptidase, an enzyme Zinc D-Ala-D-Ala carboxypeptidase, an enzyme ...
"Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2 ... Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene. Three different forms of human pancreatic ... "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)". Pascual R, Burgos FJ, Salva M, et al. (1989). "Purification and properties ... Human Carboxypeptidase A2) at the PDBe-KB. Portal: Biology v t e (Articles with short description, Short description matches ...
... intracellular carboxypeptidase of Thermoactinomycetes--a distant analog of animal carboxypeptidase]". Biokhimiia. 49 (2): 292- ... Carboxypeptidase+T at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... Carboxypeptidase T (EC 3.4.17.18, CPT) is a hydrolytic enzyme. This enzyme catalyses the following chemical reaction: Releases ... Osterman AL, Stepanov VM, Rudenskaia GN, Khodova OM, Tsaplina IA (February 1984). "[Carboxypeptidase T-- ...
... is an enzyme that in humans is encoded by the CPA1 gene. Three different forms of human pancreatic ... "Entrez Gene: CPA1 carboxypeptidase A1 (pancreatic)". Catasús L, Villegas V, Pascual R, et al. (1992). "cDNA cloning and ... Carboxypeptidase A1 is a monomeric pancreatic exopeptidase. It is involved in zymogen inhibition. GRCh38: Ensembl release 89: ... Stewart EA, Craik CS, Hake L, Bowcock AM (1990). "Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter". Am. ...
Alanine+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... Alanine carboxypeptidase (EC 3.4.17.6, N-benzoyl-L-alanine-amidohydrolase) is an enzyme. This enzyme catalyses the following ...
The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A ( ... "Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family". J. ... Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended ... Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to ...
"Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1". ... Carboxypeptidase Taq (EC 3.4.17.19) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal ... Carboxypeptidase+Taq at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... Lee SH, Taguchi H, Yoshimura E, Minagawa E, Kaminogawa S, Ohta T, Matsuzawa H (August 1994). "Carboxypeptidase Taq, a ...
Term carboxypeptidase D may refer to: Carboxypeptidase, a generic enzyme class Carboxypeptidase D, the EC 3.4.16.6 enzyme class ... the EC 3.4.17.22 enzyme class This disambiguation page lists articles associated with the title Carboxypeptidase D. If an ...
Gly-Xaa carboxypeptidase (EC 3.4.17.4, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast ... Gly-Xaa+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal amino acid from a ...
... (GCPII), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase ... All refer to the same protein glutamate carboxypeptidase II. GCPII is mainly expressed in four tissues of the body, including ... and carboxypeptidase activity based on the parent tissue. The hydrolysis of NAAG by GCPII obeys Michaelis-Menten kinetics. ...
The structure of the complex between bovine carboxypeptidase A and the 39-amino-acid carboxypeptidase A inhibitor from potatoes ... Hass GM, Nau H, Biemann K, Grahn DT, Ericsson LH, Neurath H (March 1975). "The amino acid sequence of a carboxypeptidase ... In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well- ... Rees DC, Lipscomb WN (August 1980). "Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution". Proc ...
PCI also inhibits carboxypeptidase R without affecting the activity of carboxypeptidase N in the circulation and have therefore ... May 1998). "Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor ... Potato carboxypeptidase inhibitor (PCI) is a naturally occurring protease inhibitor peptide in potatoes that can form complexes ... a Redlitz A, Tan AK, Eaton DL, Plow EF (November 1995). "Plasma carboxypeptidases as regulators of the plasminogen system". J. ...
... 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 ...
M14_CPA; Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup. pfam02244. Location:29 → 101. Propep_ ... CPA2 carboxypeptidase A2 [Homo sapiens] CPA2 carboxypeptidase A2 [Homo sapiens]. Gene ID:1358 ... carboxypeptidase A2provided by HGNC. Primary source. HGNC:HGNC:2297 See related. Ensembl:ENSG00000158516 MIM:600688; ... CPA2 carboxypeptidase A2 [ Homo sapiens (human) ] Gene ID: 1358, updated on 23-Nov-2023 ...
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View mouse Cpa2 Chr6:30541641-30564475 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Content aggregated by Proteopedia from external resources falls under the respective resources copyrights. See the Terms of Service ...
Human carboxypeptidase N (CPN), a member of the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, is an extracellular ... Arginine carboxypeptidase (CPR) is a labile enzyme present in human serum which is unrelated to carboxypeptidase N. In this ... Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in ... Kininase I-type carboxypeptidases enhance nitric oxide production in endothelial cells by generating bradykinin B1 receptor ...
SERINE CARBOXYPEPTIDASE II (bread wheat). Find diseases associated with this biological target and compounds tested against it ...
H. pylori Csd4 consists of three domains: an N-terminal D,L-carboxypeptidase domain with a typical carboxypeptidase fold, a ... It is a Zn(2+)-dependent D,L-carboxypeptidase that cleaves the bond between the γ-D-Glu and the mDAP of the non-cross-linked ... The D,L-carboxypeptidase domain recognizes the substrate by interacting primarily with the terminal mDAP moiety of the ... Structural basis for the recognition of muramyltripeptide by Helicobacter pylori Csd4, a D,L-carboxypeptidase controlling the ...
... is a recently identified zinc metalloprotease with carboxypeptidase activity that was identified using our genomics platform. ... Substrate-Based Design of the First Class of Angiotensin-Converting Enzyme-Related Carboxypeptidase (ACE2) Inhibitors. *Natalie ... Distinct roles for angiotensin-converting enzyme 2 and carboxypeptidase A in the processing of angiotensins within the murine ... Angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a recently identified zinc metalloprotease with ...
Mast cells express ETRs and can thereby be degranulated by ET-1, and mast cell proteases chymase and carboxypeptidase A3 (CPA3 ... Mouse connective tissue mast cell proteases tryptase and carboxypeptidase A3 play protective roles in itch induced by ... Mouse connective tissue mast cell proteases tryptase and carboxypeptidase A3 play protective roles in itch induced by ... Mouse connective tissue mast cell proteases tryptase and carboxypeptidase A3 play protective roles in itch induced by ...
The degradation of the GSH moieties requires the activity of the Cys-Gly carboxypeptidase GliJ, for which we describe the X-ray ...
In addition, carboxypeptidase M expression could be detected in HL-60, U937, and THP-1 myeloid cell lines. Vitamin D3-induced ... Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage ... Expression of carboxypeptidase M on mRNA level and enzymatic activity markedly increase during in vitro differentiation of ... Further studies are needed to elucidate the functional role of carboxypeptidase M during monocytic differentiation and ...
You say folate, I say folic acid… lets call the whole thing off? Paraphrasing the famous lyrics may help us remember that similar sounding words may not always translate to the same molecules! Folate has become an umbrella term used interchangeably to describe different forms of the basic vitamin B9: it can be easy to …. Folate or Folic? Read More ». ...
Note: These kits are not intended for diagnosing or treatment.
Pharmacologic class Carboxypeptidase [EPC] with pharma code N0000184013. ... NDC Products with Carboxypeptidase. The table contains 1 products whose active ingredient are classified under the same ... pharmacologic class Carboxypeptidase [EPC].. NDC. Proprietary Name. Non-Proprietary Name. Dosage Form. Route Name. Company Name ...
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.
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Category: Carboxypeptidase. Posted on September 4, 2022. Current amplitudes in both WT and KO cells improved following ...
Serine-Type D-Ala-D-Ala Carboxypeptidase*Serine-Type D-Ala-D-Ala Carboxypeptidase ... A carboxypeptidase that is specific for proteins that contain two ALANINE residues on their C-terminal. Enzymes in this class ... This graph shows the total number of publications written about "Serine-Type D-Ala-D-Ala Carboxypeptidase" by people in this ... Below are the most recent publications written about "Serine-Type D-Ala-D-Ala Carboxypeptidase" by people in Profiles. ...
... the C- Terminal Lysine of Stromal Cell-Derived Factor-1a: ... Carboxypeptidase M Expressed by Human Bone Marrow Cells Cleaves the C- Terminal Lysine of Stromal Cell-Derived Factor-1a ... Carboxypeptidase M Expressed by Human Bone Marrow Cells Cleaves the C- Terminal Lysine of Stromal Cell-Derived Factor-1a: ... Scholar articles Carboxypeptidase M expressed by human bone marrow cells cleaves the C-terminal lysine of stromal cell-derived ...
Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the ... Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the ... Recombinant Mouse Carboxypeptidase M Protein (His Tag) Beta LifeScience SKU/CAT #: BLPSN-0577 ... Recombinant Mouse Carboxypeptidase M Protein (His Tag) Beta LifeScience SKU/CAT #: BLPSN-0577 ...
Carboxypeptidase A1 derived from Recombinant full-length human CPA1 protein. Clone: CPA1/2714. Gene ID: 1357 ... Carboxypeptidase A1, Carboxypeptidase A1 (pancreatic); CPA1; Pancreatic Carboxypeptidase A1; Procarboxypeptidase A1 pancreatic ... Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys ... Carboxypeptidase A1 / CPA1 (Pancreatic Cancer Marker) [CPA1/2714]. Monoclonals Mouse Monoclonals Primary Antibodies ...
Human recombinant Carboxypeptidase A2 (CPA2), Clone: MM0122-11M21, Antibody Isotype: Mouse IgG2, Applications: A: WB-(1 to 500- ... Mouse Monoclonal anti-human Carboxypeptidase A2 (CPA2) , Size: 100ug, Immunogen: ... Home Page > ANTIBODY > MONOCLONAL ANTIBODY > Anti-Human Antibody > Mouse Monoclonal anti-human Carboxypeptidase A2 (CPA2) Mouse ... This antibody was selected for its ability to detect human Carboxypeptidase A2 (CPA2).. ...
Elastin Products Company, Inc. (EPC) warrants that its products are merchantable quality and warrants the accuracy of its description of such products. EPC warrants that the products described herein has performed as disclosed by EPC. Purchaser must determine suitability of the product for any unusual or particular purpose. THIS WARRANTY IS EXCLUSIVE AND EPC MAKES NO OTHER WARRANTY, EXPRESSED OR IMPLIED, THAT THE PRODUCT DESCRIBED HEREIN IS MERCHANTABLE OR FIT FOR ANY PARTICULAR PURPOSE. Whenever any items(s) leaves our premises, such items(s) are absolutely out of our control. EPC therefore makes no warranty as to fitness for any particular purpose or to protection against patent, copyright and trade mark infrigement. In any and all situations it is the total responsibility of the buyer and/or user to determine any and all possible patent, copyright and trade.. ...
Order Rabbit anti-human carboxypeptidase A3 mast cell polyclonal Antibody carboxypeptidase A3 03015445843 at Gentaur ...
A mutation of carboxypeptidase E (CPE), an enzyme active in the processing and sorting of prohormones, causes obesity in the ... A mutation of carboxypeptidase E (CPE), an enzyme active in the processing and sorting of prohormones, causes obesity in the ...
Carboxypeptidase inhibitor I68. crystal structure of the tick carboxypeptidase inhibitor in complex with human carboxypeptidase ... The Carboxypeptidase inhibitor I68 family represents a family of tick carboxypetidase inhibitors. ...
Gilvarg, Charles (Inventor). / NOVEL ASSAY FOR PANCREATIC PATHOLOGY --DETERMINATION OF CARBOXYPEPTIDASE A LEVELS IN HUMAN SERUM ... Dive into the research topics of NOVEL ASSAY FOR PANCREATIC PATHOLOGY --DETERMINATION OF CARBOXYPEPTIDASE A LEVELS IN HUMAN ... Gilvarg, C. (2011). NOVEL ASSAY FOR PANCREATIC PATHOLOGY --DETERMINATION OF CARBOXYPEPTIDASE A LEVELS IN HUMAN SERUM. ... NOVEL ASSAY FOR PANCREATIC PATHOLOGY --DETERMINATION OF CARBOXYPEPTIDASE A LEVELS IN HUMAN SERUM. / Gilvarg, Charles (Inventor ...
Carboxypeptidase U: a novel plasma carboxypeptidase with affinitiy for plasminogen ...
  • 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)
  • Angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a recently identified zinc metalloprotease with carboxypeptidase activity that was identified using our genomics platform. (acs.org)
  • 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)
  • A mutation of carboxypeptidase E (CPE), an enzyme active in the processing and sorting of prohormones, causes obesity in the fat/fat mouse. (nih.gov)
  • Most peptide substrates were sequentially truncated from the carboxyl-terminus revealing that this enzyme is a bona fide carboxypeptidase. (usf.edu)
  • Function This molecular model depicts the enzyme Bovine Carboxypeptidase A (CPA). (harvard.edu)
  • Human pancreatic procarboxypeptidase A exists as three different active forms, two of which are designated carboxypeptidase A1 (CPA1) and carboxypeptidase A2 (CPA2). (neobiotechnologies.com)
  • This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse immunized with human recombinant protein of Carboxypeptidase A2 (CPA2). (angioproteomie.com)
  • This antibody was selected for its ability to detect human Carboxypeptidase A2 (CPA2). (angioproteomie.com)
  • It is a Zn(2+)-dependent D,L-carboxypeptidase that cleaves the bond between the γ-D-Glu and the mDAP of the non-cross-linked muramyltripeptide (muramyl-L-Ala-γ-D-Glu-mDAP) of the peptidoglycan to produce the muramyldipeptide (muramyl-L-Ala-γ-D-Glu) and mDAP. (rcsb.org)
  • Description Carboxypeptidase M (CPM) is a membrane-bound zinc-dependent protease that cleaves C-terminal basic residues, such as arginine or lysine, from peptides/proteins. (razikurd.ir)
  • Glutamate carboxypeptidase II (GCPII, EC 3.4.17.21) is a membrane peptidase expressed in a number of tissues such as kidney, prostate and brain. (johnshopkins.edu)
  • In this paper we report expression of an extracellular portion of human glutamate carboxypeptidase II (amino acids 44-750) in Drosophila Schneider's cells and its purification to homogeneity. (johnshopkins.edu)
  • Glutamate carboxypeptidase II gene polymorphisms and neural tube defects in a high-risk Chinese population. (cdc.gov)
  • Ghrelin regulates hypothalamic prolyl carboxypeptidase expression in m" by Jin Kwon Jeong, Jung Dae Kim et al. (gwu.edu)
  • Characterization of PdCP1, a serine carboxypeptidase from Pseudogymnoa" by Chapman Beekman, Zhenze Jiang et al. (usf.edu)
  • Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. (wikipedia.org)
  • Analysis of Protein Array containing more than 19,000 full-length human proteins using Carboxypeptidase A1 / CPA1 Mouse Monoclonal Antibody (CPA1/2714). (neobiotechnologies.com)
  • ACE-2 is the SARS-CoV and SARS-CoV2 Spike protein receptor in vivo (4-6), functions catalytically as a carboxypeptidase to cleave several substrates including angiotensins I and II, and acts as a partner for B0AT1-family amino acid transporters (1, 2). (rndsystems.com)
  • Carboxypeptidases that cleave positively charged amino acids (arginine, lysine) are called carboxypeptidase B (B for basic). (wikipedia.org)
  • Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the carboxypeptidases family. (betalifesci.com)
  • Initial studies on carboxypeptidases focused on pancreatic carboxypeptidases A1, A2, and B in the digestion of food. (wikipedia.org)
  • Western Blot Analysis of pancreatic tissue lysate using Carboxypeptidase A1 / CPA1 Mouse Monoclonal Antibody (CPA1/2714). (neobiotechnologies.com)
  • Pyrrolidone carboxypeptidases (Pcps) (E.C. 3.4.19.3) can cleave the peptide bond adjacent to pyro-glutamic acid (pGlu), an N-terminal modification observed in some proteins that provides protection against common proteases. (leehicam.com)
  • Dive into the research topics of 'The pro region is not required for the expression or intracellular routeing of carboxypeptidase E'. Together they form a unique fingerprint. (elsevierpure.com)
  • Mouse connective tissue mast cell proteases tryptase and carboxypeptidase A3 play protective roles in itch induced by endothelin-1. (iasp-pain.org)
  • Mast cells express ETRs and can thereby be degranulated by ET-1, and mast cell proteases chymase and carboxypeptidase A3 (CPA3) are known to either generate or degrade ET-1, respectively, suggesting a role for mast cell proteases in the regulation of ET-1-induced itch. (iasp-pain.org)
  • They also regulate biological processes, such as the biosynthesis of neuroendocrine peptides such as insulin requires a carboxypeptidase. (wikipedia.org)
  • Carboxypeptidases hydrolyze peptides at the first amide or polypeptide bond on the C-terminal end of the chain. (wikipedia.org)
  • Carboxypeptidases are usually classified into one of several families based on their active site mechanism. (wikipedia.org)
  • This mechanism ensures that the cells wherein pro-carboxypeptidase A is produced are not themselves digested. (wikipedia.org)
  • 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 act by replacing the substrate water with a carbonyl (C=O) group. (wikipedia.org)
  • Another classification system for carboxypeptidases refers to their substrate preference. (wikipedia.org)
  • The D,L-carboxypeptidase domain recognizes the substrate by interacting primarily with the terminal mDAP moiety of the muramyltripeptide. (rcsb.org)
  • A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. (rush.edu)
  • Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the surface of specialized cells and tissues in the human body. (betalifesci.com)
  • Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (PubMed:8806703). (neobiotechnologies.com)
  • A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. (bvsalud.org)
  • Formalin-fixed, paraffin-embedded human Pancreas stained with Carboxypeptidase A1 / CPA1 Mouse Monoclonal Antibody (CPA1/2714). (neobiotechnologies.com)
  • 1990. Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter. (neobiotechnologies.com)
  • In addition, carboxypeptidase M expression could be detected in HL-60, U937, and THP-1 myeloid cell lines. (uni-regensburg.de)
  • Vitamin D3-induced monocytic differentiation resulted in an increased carboxypeptidase M expression in all three cell lines. (uni-regensburg.de)
  • Enzymes that use a metal in the active site are called "metallo-carboxypeptidases" (EC number 3.4.17). (wikipedia.org)
  • Other carboxypeptidases that use active site serine residues are called "serine carboxypeptidases" (EC number 3.4.16). (wikipedia.org)
  • Those that use an active site cysteine are called "cysteine carboxypeptidase" (or "thiol carboxypeptidases")(EC number 3.4.18). (wikipedia.org)
  • The table contains 1 products whose active ingredient are classified under the same pharmacologic class Carboxypeptidase [EPC]. (ndclist.com)
  • SDS-PAGE Analysis Purified Carboxypeptidase A1 / CPA1 Mouse Monoclonal Antibody (CPA1/2714). (neobiotechnologies.com)
  • The degradation of the GSH moieties requires the activity of the Cys-Gly carboxypeptidase GliJ, for which we describe the X-ray structure here. (cipsm.de)
  • Further studies are needed to elucidate the functional role of carboxypeptidase M during monocytic differentiation and activation. (uni-regensburg.de)
  • This graph shows the total number of publications written about "Carboxypeptidase B" by people in this website by year, and whether "Carboxypeptidase B" was a major or minor topic of these publications. (rush.edu)