A metallocarboxypeptidase that removes C-terminal lysine and arginine from biologically active peptides and proteins thereby regulating their activity. It is a zinc enzyme with no preference shown for lysine over arginine. Pro-carboxypeptidase U in human plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.
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 184.108.40.206 and EC 220.127.116.11.
Glutamate Carboxypeptidase II
Amino Acid Sequence
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Serine-Type D-Ala-D-Ala Carboxypeptidase
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.
Serum peptides derived from certain cleaved COMPLEMENT PROTEINS during COMPLEMENT ACTIVATION. They induce smooth MUSCLE CONTRACTION; mast cell HISTAMINE RELEASE; PLATELET AGGREGATION; and act as mediators of the local inflammatory process. The order of anaphylatoxin activity from the strongest to the weakest is C5a, C3a, C4a, and C5a des-arginine.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
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.
Saccharomyces cerevisiae Proteins
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).
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.
Ribonucleoprotein, U1 Small Nuclear
A nuclear RNA-protein complex that plays a role in RNA processing. In the nucleoplasm, the U1 snRNP along with other small nuclear ribonucleoproteins (U2, U4-U6, and U5) assemble into SPLICEOSOMES that remove introns from pre-mRNA by splicing. The U1 snRNA forms base pairs with conserved sequence motifs at the 5'-splice site and recognizes both the 5'- and 3'-splice sites and may have a fundamental role in aligning the two sites for the splicing reaction.
Protein Processing, Post-Translational
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidase activity on some substrates. (From Enzyme Nomenclature, 1992) EC 18.104.22.168.
Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. (1/124)BACKGROUND: Procarboxypeptidase U (proCPU) is a novel proenzyme found in human plasma. The active form, carboxypeptidase U (CPU; EC 22.214.171.124), retards the rate of fibrinolysis through its ability to cleave C-terminal lysine residues on fibrin partially degraded by plasmin. This reduces the number of high-affinity plasminogen-binding sites on fibrin. METHODS: We developed an assay to determine the proCPU concentration in human plasma. The assay involved quantitative conversion of proCPU to active CPU by thrombin-thrombomodulin, a very efficient activator of proCPU, followed by determination of the enzymatic activity of CPU with the substrate hippuryl-L-arginine, using an HPLC-assisted determination of the released hippuric acid. Using this method, we established a reference interval based on 490 healthy individuals. RESULTS: The mean proCPU concentration, determined after activation of the zymogen in diluted plasma and expressed as CPU activity, was 964 U/L, with a SD of 155 U/L. The population showed a gaussian distribution. However, we noticed important differences related to age and the use of hormone preparations. CONCLUSIONS: The sensitivity and precision of the method make it suitable for routine clinical determinations and as a reference procedure. (+info)
Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains. (2/124)A collection of 56 purified thrombin mutants, in which 76 charged or polar surface residues on thrombin were mutated to alanine, was used to identify key residues mediating the interactions of thrombin with thrombomodulin (TM), protein C, and thrombin-activatable fibrinolysis inhibitor (TAFI). Comparison of protein C activation in the presence and absence of TM identified 11 residues mediating the thrombin-TM interaction (Lys(21), Gln(24), Arg(62), Lys(65), His(66), Arg(68), Thr(69), Tyr(71), Arg(73), Lys(77), Lys(106)). Three mutants (E25A, D51A, R89A/R93A/E94A) were found to have decreased ability to activate TAFI yet retained normal protein C activation, whereas three other mutants (R178A/R180A/D183A, E229A, R233A) had decreased ability to activate protein C but maintained normal TAFI activation. One mutant (W50A) displayed decreased activation of both substrates. Mapping of these functional residues on thrombin revealed that the 11 residues mediating the thrombin-TM interaction are all located in exosite I. Residues important in TAFI activation are located above the active-site cleft, whereas residues involved in protein C are located below the active-site cleft. In contrast to the extensive overlap of residues mediating TM binding and fibrinogen clotting, these data show that distinct domains in thrombin mediate its interactions with TM, protein C, and TAFI. These studies demonstrate that selective enzymatic properties of thrombin can be dissociated by site-directed mutagenesis. (+info)
A novel approach to arterial thrombolysis. (3/124)Achieving early, complete, and sustained reperfusion after acute myocardial infarction does not occur in approximately 50% of patients, even with the most potent established thrombolytic therapy. Bleeding is observed with increased concentrations of thrombolytics as well as with adjunctive antithrombotic and antiplatelet agents. A novel approach to enhance thrombolytic therapy is to inhibit the activated form of thrombin-activatable fibrinolysis inhibitor (TAFI), which attenuates fibrinolysis in clots formed from human plasma. Identification of TAFI in rabbit plasma facilitated the development of a rabbit arterial thrombolysis model to compare the thrombolytic efficacy of tissue-plasminogen activator (tPA) alone or with an inhibitor, isolated from the potato tuber (PTI), of activated TAFI (TAFIa). Efficacy was assessed by determining the time to patency, the time the vessel remained patent, the maximal blood flow achieved during therapy, the percentage of the original thrombus, which lysed, the percentage change in clot weight, the net clot accreted, and the release of radioactive fibrin degradation products into the circulation. The results indicate that coadministration of PTI and tPA significantly improved tPA-induced thrombolysis without adversely affecting blood pressure, activated partial thromboplastin time, thrombin clotting time, fibrinogen, or alpha-2-antiplasmin concentrations. The data indicate that inhibitors of TAFIa may comprise novel and very effective adjuncts to tPA and improve thrombolytic therapy to achieve both clot lysis and vessel patency. (+info)
Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. (4/124)Thrombin-activable fibrinolysis inhibitor (TAFI) is present in the circulation as an inactive zymogen. Thrombin converts TAFI to a carboxypeptidase B-like enzyme (TAFIa) by cleaving at Arg(92) in a process accelerated by the cofactor, thrombomodulin. TAFIa attenuates fibrinolysis. TAFIa can be inactivated by both proteolysis by thrombin and spontaneous temperature-dependent loss of activity. The identity of the thrombin cleavage site responsible for loss of TAFIa activity was suggested to be Arg(330), but site-directed mutagenesis of this residue did not prevent inactivation of TAFIa by thrombin. In this study we followed TAFI activation and TAFIa inactivation by thrombin/thrombomodulin in time and characterized the cleavage pattern of TAFI using matrix-assisted laser desorption ionization mass spectrometry. Mass matching of the fragments revealed that TAFIa was cleaved at Arg(302). Studies of a mutant R302Q-TAFI confirmed identification of this thrombin cleavage site and, furthermore, suggested that inactivation of TAFIa is based on its conformational instability rather than proteolytic cleavage at Arg(302). (+info)
Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. (5/124)We have used site-directed mutagenesis and a recombinant expression system for thrombin-activable fibrinolysis inhibitor (TAFI) in order to identify the thrombin cleavage site in activated TAFI (TAFIa) and to determine the relative contribution of proteolytic cleavage and thermal instability in regulation of TAFIa activity in clots. Arg-330 of TAFIa had been proposed to be the thrombin cleavage site based on studies with trypsin, but mutation of this residue to Gln did not prevent thrombin-mediated cleavage nor did mutation to Gln of the nearby Arg-320 residue. However, mutation of Arg-302 to Gln abolished thrombin-mediated cleavage of TAFIa. All TAFIa variants were susceptible to plasmin cleavage. Interestingly, all Arg to Gln substitutions decreased the thermal stability of TAFIa. The antifibrinolytic potential of the TAFI mutants in vitro correlates with the thermal stability of their respective TAFIa species, indicating that this property plays a key role in regulating the activity if TAFIa. Incubation of TAFIa under conditions that result in complete thermal inactivation of the enzyme accelerates subsequent thrombin- and plasmin-mediated cleavage of TAFIa. Moreover, the extent of cleavage of TAFIa by thrombin does not affect the rate of decay of TAFIa activity. Collectively, these studies point to a role for the thermal instability, but not for proteolytic cleavage, of TAFIa in regulation of its activity and, thus, of its antifibrinolytic potential. Finally, we propose a model for the thermal instability of TAFIa. (+info)
Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. (6/124)Thrombin activatable fibrinolysis inhibitor (TAFI, or procarboxypeptidase B) is the precursor of a recently described carboxypeptidase that potently attenuates fibrinolysis. Therefore, we hypothesized that elevated plasma TAFI levels induce a hypofibrinolytic state associated with an increased risk for venous thrombosis. To evaluate this hypothesis, we developed an electroimmunoassay for TAFI antigen and used this assay to measure TAFI levels in the Leiden Thrombophilia Study, a case-control study of venous thrombosis in 474 patients with a first deep vein thrombosis and 474 age- and sex-matched control subjects. In 474 healthy control subjects, an increase of TAFI with age was observed in women but not in men. Oral contraceptive use also increased the TAFI concentration. TAFI levels above the 90th percentile of the controls (> 122 U/dL) increased the risk for thrombosis nearly 2-fold compared with TAFI levels below the 90th percentile (odds ratio, 1.7; 95% confidence interval, 1.1-2.5). Adjustment for various possible confounders did not materially affect this estimate. These results indicate that elevated TAFI levels form a mild risk factor for venous thrombosis. Such levels were found in 9% of healthy controls and in 14% of patients with a first deep vein thrombosis. Elevated TAFI levels did not enhance the thrombotic risk associated with factor V Leiden but may interact with high factor VIII levels. (Blood. 2000;95:2855-2859) (+info)
Elements of the primary structure of thrombomodulin required for efficient thrombin-activable fibrinolysis inhibitor activation. (7/124)Deletion and point mutants of soluble thrombomodulin were used to compare and contrast elements of primary structure required for the activation of thrombin-activable fibrinolysis inhibitor (TAFI) and protein C. The smallest mutant capable of efficiently promoting TAFI activation contained residues including the c-loop of epidermal growth factor-3 (EGF3) through EGF6. This mutant is 13 residues longer than the smallest mutant that functioned well with protein C; the latter consisted of residues from the interdomain loop connecting EGF3 and EGF4 through EGF6. Alanine point mutants showed no loss of function in protein C activation for mutations within the c-loop of EGF3. In TAFI activation, however, alanine mutations cause a 50% reduction at Tyr-337, 67% reductions at Asp-338 and Leu-339, and 90% or greater reductions at Val-340, Asp-341, and Glu-343. A mutation at Asp-349 in the peptide connecting EGF3 to EGF4 eliminated activity against both TAFI and protein C. Oxidation of Met-388 in the peptide connecting EGF5 to EGF6 reduced the rate of protein C activation by 80% but marginally, if at all, affected the rate of TAFI activation. Mutation at Phe-376 severely reduced protein C activation but only marginally influenced that of TAFI. A Q387P mutation, however, severely reduced both activities. TAFI activation was shown to be Ca(2+)-dependent. The response, unlike that of protein C, was monotonic and was half-maximal at 0.25 mm Ca(2+). Like protein C activation, TAFI activation was eliminated by a monoclonal antibody directed at the thrombin-binding domain (EGF5) but was not affected by one directed at EGF2. Thus, elements of structure in the thrombin-binding domain are needed for the activation of both protein C and TAFI, but more of the primary structure is needed for TAFI activation. In addition, some residues are needed for one of the reactions but not the other. (+info)
Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not. (8/124)Carboxypeptidase R (EC 126.96.36.199; CPR) and carboxypeptidase N (EC 3. 4.17.3; CPN) cleave carboxyl-terminal arginine and lysine residues from biologically active peptides such as kinins and anaphylatoxins, resulting in regulation of their biological activity. Human proCPR, also known as thrombin-activatable fibrinolysis inhibitor, plasma pro-carboxypeptidase B, and pro-carboxypeptidase U, is a plasma zymogen activated during coagulation. CPN, however, previously termed kininase I and anaphylatoxin inactivator, is present in a stable active form in plasma. We report here the isolation of mouse proCPR and CPN cDNA clones that can induce their respective enzymatic activities in culture supernatants of transiently transfected cells. Potato carboxypeptidase inhibitor can inhibit carboxypeptidase activity in culture medium of mouse proCPR-transfected cells. The expression of proCPR mRNA in murine liver is greatly enhanced following LPS injection, whereas CPN mRNA expression remains unaffected. Furthermore, the CPR activity in plasma increased 2-fold at 24 h after LPS treatment. Therefore, proCPR can be considered a type of acute phase protein, whereas CPN is not. An increase in CPR activity may facilitate rapid inactivation of inflammatory mediators generated at the site of Gram-negative bacterial infection and may consequently prevent septic shock. In view of the ability of proCPR to also inhibit fibrinolysis, an excess of proCPR induced by LPS may contribute to hypofibrinolysis in patients suffering from disseminated intravascular coagulation caused by sepsis. (+info)
... 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 US 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 US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.16). ...
... (EC 188.8.131.52, 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 US 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 184.108.40.206, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L- ... Folk JE (1970). "Carboxypeptidase B (porcine pancreas)". Methods Enzymol. 19: 504-508. doi:10.1016/0076-6879(70)19036-7. ... Wallace EF, Evans CJ, Jurik SM, Mefford IN, Barchas JD (1982). "Carboxypeptidase B activity from adrenal medulla--is it ... The MEROPS online database for peptidases and their inhibitors: M14.003 Carboxypeptidase+B at the US 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 US 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 220.127.116.11, 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 US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ...
... (EC 18.104.22.168, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ... Carboxypeptidase+C at the US 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 22.214.171.124. The first number in an EC number indicates the main class that the enzyme ... Lysine carboxypeptidase (EC 126.96.36.199) 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 ...
... (EC 188.8.131.52, CPM) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of C- ... Carboxypeptidase+M at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... 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 (Genes on human chromosome 7, EC 3.4.17, All stub articles, ...
... intracellular carboxypeptidase of Thermoactinomycetes--a distant analog of animal carboxypeptidase]". Biokhimiia. 49 (2): 292- ... Carboxypeptidase T (EC 184.108.40.206, CPT) is an enzyme. This enzyme catalyses the following chemical reaction: Releases a C- ... Carboxypeptidase+T at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... 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 US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.17). ... Alanine carboxypeptidase (EC 220.127.116.11, 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 18.104.22.168) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal ... Carboxypeptidase+Taq at the US National Library of Medicine Medical Subject Headings (MeSH) 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 ...
Carboxypeptidase D (disambiguation)
Term carboxypeptidase D may refer to: Carboxypeptidase, a generic enzyme class Carboxypeptidase D, the EC 22.214.171.124 enzyme class ... the EC 126.96.36.199 enzyme class This disambiguation page lists articles associated with the title Carboxypeptidase D. If an ...
Gly-Xaa carboxypeptidase (EC 188.8.131.52, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast ... Gly-Xaa+carboxypeptidase at the US 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 ...
Glutamate carboxypeptidase II
... (GCPII), also known as N-acetyl-L-aspartyl-L-glutamate peptidase I (NAALADase I), NAAG peptidase ... All of which refer to the same protein glutamate carboxypeptidase II. GCPII is mainly expressed in four tissues of the body, ... and carboxypeptidase activity based on the parent tissue. The hydrolysis of NAAG by GCPII obeys Michaelis-Menten kinetics. ...
Carboxypeptidase A inhibitor
The structure of the complex between bovine carboxypeptidase A and the 39-amino-acid carboxypeptidase A inhibitor from potatoes ... Hass GM, Nau H, Biemann K, Grahn DT, Ericsson LH, Neurath H (March 1975). "The amino acid sequence of a carboxypeptidase ... In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well- ... Rees DC, Lipscomb WN (August 1980). "Structure of the potato inhibitor complex of carboxypeptidase A at 2.5-A resolution". Proc ...
Potato carboxypeptidase inhibitor
PCI also inhibits carboxypeptidase R without affecting the activity of carboxypeptidase N in the circulation and have therefore ... May 1998). "Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor ... Potato carboxypeptidase inhibitor (PCI) is a naturally occurring protease inhibitor peptide in potatoes that can form complexes ... a Redlitz A, Tan AK, Eaton DL, Plow EF (November 1995). "Plasma carboxypeptidases as regulators of the plasminogen system". J. ...
Molecular characterization of human intestinal folylpoly-gamma-glutamate carboxypeptidase (FGCP) and mutation associated with...
Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of...
To study the role of different carboxypeptidases in lepidopteran protein digestion, the effect of potato carboxypeptidase ... To study the role of different carboxypeptidases in lepidopteran protein digestion, the effect of potato carboxypeptidase ... To study the role of different carboxypeptidases in lepidopteran protein digestion, the effect of potato carboxypeptidase ... To study the role of different carboxypeptidases in lepidopteran protein digestion, the effect of potato carboxypeptidase ...
Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors :: MPG.PuRe
Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors ... Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors Bayes, A., Comellas-Bigler, M., ... 2005). Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors. Proceedings of the ...
Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. - Oxford...
... polyglutamylated folates which are digested to monoglutamyl folates by the action of folylpoly-gamma-glutamate carboxypeptidase ... Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. ... Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. ... Aged, Alleles, Alternative Splicing, Animals, Antigens, Surface, COS Cells, Carboxypeptidases, Cloning, Molecular, DNA ...
Mapping of the active site of glutamate carboxypeptidase II by site-directed mutagenesis<...
N2 - Human glutamate carboxypeptidase II [GCPII (EC 184.108.40.206)] is recognized as a promising pharmacological target for the ... AB - Human glutamate carboxypeptidase II [GCPII (EC 220.127.116.11)] is recognized as a promising pharmacological target for the ... Human glutamate carboxypeptidase II [GCPII (EC 18.104.22.168)] is recognized as a promising pharmacological target for the ... Mapping of the active site of glutamate carboxypeptidase II by site-directed mutagenesis. In: FEBS Journal. 2007 ; Vol. 274, No ...
Discovery of Orally Available Prodrugs of the Glutamate Carboxypeptidase II (GCPII) Inhibitor 2-Phosphonomethylpentanedioic...
Dive into the research topics of Discovery of Orally Available Prodrugs of the Glutamate Carboxypeptidase II (GCPII) Inhibitor ... 2-Phosphonomethylpentanedioic acid (1, 2-PMPA) is a potent inhibitor of glutamate carboxypeptidase II which has demonstrated ... abstract = "2-Phosphonomethylpentanedioic acid (1, 2-PMPA) is a potent inhibitor of glutamate carboxypeptidase II which has ... N2 - 2-Phosphonomethylpentanedioic acid (1, 2-PMPA) is a potent inhibitor of glutamate carboxypeptidase II which has ...
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Low-dose carboxypeptidase-G2 for methotrexate toxicity in a child. Pediatr Blood Cancer. 2010 Dec 15; 55(7):1439-40. ... Three new prodrugs for suicide gene therapy using carboxypeptidase G2 elicit bystander efficacy in two xenograft models. Cancer ... Regressions of established breast carcinoma xenografts by carboxypeptidase G2 suicide gene therapy and the prodrug CMDA are due ... Liquid chromatography-tandem mass spectrometry (LC-MS-MS) method for monitoring methotrexate in the setting of carboxypeptidase ...
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MESH TREE NUMBER CHANGES - 2008 MeSH
Robert Caesar | University of Gothenburg
Professor David Parkinson - University of Plymouth
Expression of carboxypeptidase-H and insulin but not glutamate decarboxylase on the beta-cell surface Diabetes 43, (3) 418-425 ... Parkinson D (1992) Carboxypeptidase H in bovine pituitary gland: Soluble forms are not processed at the C-terminus Molecular ... Fiedorek FT & Parkinson D (1992) Carboxypeptidase H processing and secretion in rat clonal beta-cell lines Endocrinology 131 ... MAINS RE, ZHOU AN & PARKINSON D (2006) The Biosynthetic Processing and Secretion of Endogenous Carboxypeptidase H in Mouse ...
Publications - Universität Ulm
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Systematic Review for the 2017 ACC/AHA/AAPA/ABC/ACPM/AGS/APhA/ASH/ASPC/NMA/PCNA Guideline for the Prevention, Detection,...
Dive into the research topics of Systematic Review for the 2017 ACC/AHA/AAPA/ABC/ACPM/AGS/APhA/ASH/ASPC/NMA/PCNA Guideline for the Prevention, Detection, Evaluation, and Management of High Blood Pressure in Adults: A Report of the American College of Cardiology/American Heart Association Task Force on Clinical Practice Guidelines. Together they form a unique fingerprint. ...
CoP: Co-expressed Biological Processes
SMART: TBC domain annotation
Joyce Wong | Chobanian & Avedisian School of Medicine
- Molecular characterization of human intestinal folylpoly-gamma-glutamate carboxypeptidase (FGCP) and mutation associated with low folate status. (ox.ac.uk)
- Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. (ox.ac.uk)
- Dietary folates are a mixture of polyglutamylated folates which are digested to monoglutamyl folates by the action of folylpoly-gamma-glutamate carboxypeptidase (FGCP), an enzyme that is anchored to the intestinal brush border membrane and is expressed by the glutamate carboxypepidase II (GCPII) gene. (ox.ac.uk)
- Human glutamate carboxypeptidase II [GCPII (EC 22.214.171.124)] is recognized as a promising pharmacological target for the treatment and imaging of various pathologies, including neurological disorders and prostate cancer. (uthscsa.edu)
- 2-Phosphonomethylpentanedioic acid (1, 2-PMPA) is a potent inhibitor of glutamate carboxypeptidase II which has demonstrated robust neuroprotective efficacy in many neurological disease models. (johnshopkins.edu)
- Association of glutamate carboxypeptidase II (GCPII) haplotypes with breast and prostate cancer risk. (cdc.gov)
Form a unique fingerprint1
- Dive into the research topics of 'Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypeptidase B'. Together they form a unique fingerprint. (uab.cat)
- The H. zea carboxypeptidase B enzyme (CPBHz) was purified from gut content by affinity chromatography. (uab.cat)
- To study the role of different carboxypeptidases in lepidopteran protein digestion, the effect of potato carboxypeptidase inhibitor (PCI) on the digestive system of larvae of the pest insect Helicoverpa zea was investigated, and compared to that of Soybean Kunitz Trypsin Inhibitor. (uab.cat)
- Protein is dissolved in a similar way: acid protease cuts the protein into peptides (amino acid clusters), then acid carboxypeptidase cuts it into amino acid molecules. (sakeexperiencejapan.com)
- abstract = "Carboxypeptidase activity participates in the protein digestion process in the gut of lepidopteran insects, supplying free amino-acids to developing larvae. (uab.cat)
- Vishwanath N, Monis WJ, Hoffmann GA, Ramachandran B, DiGiacomo V, Wong JY, Smith ML, Layne MD. Mechanisms of aortic carboxypeptidase-like protein secretion and identification of an intracellularly retained variant associated with Ehlers-Danlos syndrome. (bu.edu)
- ACE2 is a carboxypeptidase that shares significant homologue with ACE. (origene.com)
- A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. (bvsalud.org)
- Three new prodrugs for suicide gene therapy using carboxypeptidase G2 elicit bystander efficacy in two xenograft models. (harvard.edu)
- Exoenzymes (glucoamylase, acid carboxypeptidase) cut them only at both ends. (sakeexperiencejapan.com)
- Analysis of carboxypeptidase activity in the guts showed that ingested PCI remained active in the gut, and completely inhibited the activity of carboxypeptidases A and O. Interestingly, carboxypeptidase B activity was not affected by PCI. (uab.cat)
- Analysis of several lepidopteran species showed the presence of carboxypeptidase B activity resistant to PCI in most of them. (uab.cat)
- The tubulin carboxypeptidase activity of vasohibin causes detyrosination of alpha-tubulin and may play an important role in the regulation of various phenomena. (bvsalud.org)
- Regressions of established breast carcinoma xenografts by carboxypeptidase G2 suicide gene therapy and the prodrug CMDA are due to a bystander effect. (harvard.edu)
- Carboxypeptidase Y (CPY) inhibitor, IC, shows no homology to any other known proteinase inhibitors and rather belongs to the phosphatidylethanolamine-binding protein (PEBP) family. (nih.gov)
- Furthermore, the dual prolyl carboxypeptidase (PCP)-prolyl endopeptidase (PEP) inhibitor Z-prolyl-prolinal reduced ANG-(1-7) formation in ACE2 KO mice, while the ACE2 inhibitor MLN-4760 had no effect. (nih.gov)
- Carboxypeptidase B1 is a highly tissue-specific protein and is a useful serum marker for acute pancreatitis and dysfunction of pancreatic transplants. (nih.gov)
- The technology from the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD), describes that direct administration of an adenovirus carrying the Carboxypeptidase E (CPE) gene to the hippocampus results in overexpression of the CPE protein in an experimental mouse model of AD. (nih.gov)
- 5. Glucarpidase (carboxypeptidase g2) intervention in adult and elderly cancer patients with renal dysfunction and delayed methotrexate elimination after high-dose methotrexate therapy. (nih.gov)
- 13. [Carboxypeptidase-G2 administration after high-dose methotrexate. (nih.gov)
- VORAXAZE is a carboxypeptidase indicated to reduce toxic plasma methotrexate concentration (greater than 1 micromole per liter) in adult and pediatric patients with delayed methotrexate clearance (plasma methotrexate concentrations greater than 2 standard deviations of the mean methotrexate excretion curve specific for the dose of methotrexate administered) due to impaired renal function. (nih.gov)