Inhibitors carboxypeptidase

Bayes, A., de la Vega, M. R., Vendrell, J., Aviles, F. X., Jongsma, M. A., Beekwilder, J. (2006). Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypeptidase B. Insect Biochem. Mol. Biol., 36,654-664. 

Blanco-Aparicio, C., Molina, M. A., Femandez-Salas, E., Frazier, M. L., Mas, J. M., Querol, E., Aviles, F. X., de Llorens, R. (1998). Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor cell growth. J. Biol. Chem., 273, 12370-12377. 

Wang, X., Smith, P. L., Hsu, M. -Y, Ogletree, M. L., Schumacher, W. A. (2006). Murine model of ferric chloride-induced vena cava thrombosis evidence for effect of potato carboxypeptidase inhibitor. J. Thromb. Haemost., 4, 403 10. 

Nilges, M., Gronenborn, A. M., Brunger, A. T. and Clore, G M. (1988). Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38. 

M. anisopliae carboxipeptidase carboxypeptidase 30 9.97 DIFP, 1,10-phenan-throline, potato carboxypeptidase inhibitor St. Leger etal. (1994b)... 

Several plant proteins have been isolated that inhibit the metalloprotease carboxypeptidase A [205-217] (Table 7), notably potato carboxypeptidase inhibitor PCI [207-217] (Table 7). PCI is a small, cysteine-rich protein with a compact knotted structure determined by 3 disulphide links. The C-terminal region inserts into the active site of the carboxypeptidase. The C-terminal glycine is cleaved and remains trapped in the active site, this representing an example of suicide inactivation [207-216]. 

Solanum tuberosum (potato) (Solanaceae) Potato carboxypeptidase inhibitor (PCI) (= PCIA [Pg.596]

M. Nilges, A. M. Gronenborn, A. T. Brunger, and G. M. Clore, Protein Engin., 2,27 (1988). Determination of Three-Dimensional Structures of Proteins by Simulated Annealing with Interproton Distance Restraints. Application to Crambin, Potato Carboxypeptidase Inhibitor, and Barley Serine Proteinase Inhibitor 2. 

Interproton Distance Restraints. Application to Crambin, Potato Carboxypeptidase Inhibitor, and Barley Serine Proteinase Inhibitor 2. 

Solanum PCI (= Potato Carboxypeptidase Inhibitor) (4kDa protein)... 

The metalloprotease carboxypeptidase catalyses the removal of C-terminal residues and is structurally related to the PM-located epidermal growth factor (EGF) receptor tyrosine kinase (see Chapter 8). Several plant carboxypeptidase inhibitor proteins have been characterized and the potato carboxypeptidase inhibitor (PCI) is also an EGF receptor antagonist (Table 13.4). 

Solanum Carboxypeptidase inhibitor (= PCI) Solanum tuberosum (potato) (Solanaceae) [tuber] CPA [2 nMJ [ EGF-R antagonist]... 

The potato metallocarboxypeptidase inhibitor (and metallo-carboxypeptidase inhibitors from leeches and ticks) inhibit car-boxypeptidase B after a proteolytic processing event. These... 

CARBOXYPEPTIDASE INHIBITORS act against various members of carboxypeptidase enzyme family that cleave the C-terminal residue from oligopeptides or from proteins. 

Other classes include aldehyde dehydrogenase inhibitors aldose reductase inhibitors aminopeptidase inhibitors aromatase inhibitors carboxypeptidase inhibitors cyclooxygenase inhibitors dihydrofolate... 

Other members of the metalloprotease family cleave oligopeptides (arbitrarily defined as having less than 50 amino acid residues) and do not necessarily act on proteins. These include a number of neuropeptidases of special interest and a number are discussed elsewhere. See ACE inhibitors aminopeptidase inhibitors carboxypeptidase inhibitors endopeptidase inhibitors neutral endopeptidase inhibitors. 

Peptidases. Others members of the serine protease family, cleave oligopeptides and do not necessarily act on proteins. These include two peptidases of particular interest (dipeptidylpeptidase IV and proline endopeptidase). See also AMINOPEPTIDASE INHIBITORS CARBOXYPEPTIDASE INHIBITORS ... 

Fig. 2. Effect of concentration of inhibitors on carboxypeptidase activity, following preincubation. Preincubation conditions Carboxypeptidase inhibitor, pH 7.5, 0°C., 60 minutes. Activity measurements 0.02 M CGP in veronal buffer containing 0.1 M NaCl, pH 7.5, 25°C. Activities were expressed as apparent proteolytic coefficients calculated from the strictly linear portions of first-order reaction plots.

Homandberg, G. A., Litwiller, R. D. and Peanasky, R. J. (1989) Carboxypeptidase inhibitors from Ascaris suum the primary structure. Arch. Biochem. Biophys. 270 153-161. 

Fig. 3.27. Gas chromatogram of a mixture of O-trimethylsilylated trifluoro-dideuteroethyl polyamino alcohol derivatives from a limited acid hydrolysis of 1.0 fimol of the amino terminal peptides from the carboxypeptidase inhibitor of potatoes. Reproduced from [S14] with permission of Academic Press.

Discussion of various strategies in the peptide structural work through the gas-phase methods is beyond the scope of this chapter. Sensitivity and accuracy of identification are the most important assets of such techniques. An example of the peptide GC is shown in Fig. 3.27, where a profile of O-trimethylsilylated trifluoro-dideuteroethyl polyamino alcohols is eluted at relatively high column temperature [511] the sample was obtained from the carboxypeptidase inhibitor of potatoes. 

Oral administration of D-phenylalanine, a carboxypeptidase inhibitor, was found to be of benefit in patients with certain chronic pain complaints the drug was most effective after 3-5 weeks of therapy. ... 

Ryan. C.A. Hass. G.M. Kuhn. R.W. Purification and properties of a carboxypeptidase inhibitor from potatoes. J. Biol. Chem. 1974. 249, 5495-5499. 

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