carboxypeptidase B

This is an abbreviated version!
For detailed information about carboxypeptidase B, go to the full flat file.

Word Map on EC


preferential release of a C-terminal lysine or arginine amino acid =


More, TAFI, EC, EC, protaminase, carboxypeptidase BII, CPB, Cbp, 47 kDa zymogen granule membrane associated protein, Pancreas-specific protein, PASP, ZAP47, PCB, CPB1, thrombin-activatable fibrinolysis inhibitor, HBCPB, PcpB, aCAP, tissue carboxypeptidase B, basic carboxypeptidase, pp-CpB, B carboxypeptidase, CPBAg1, CPB2, carboxypeptidase B, thrombin-activatable procarboxypeptidase B, Carboxypeptidase B1, HzCPB, cpbAs1, ppCPB, carboxypeptidase B2


     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
       carboxypeptidase B


Crystallization on EC - carboxypeptidase B

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recombinant enzyme in complex with tick carboxypeptidase inhibitor, sitting drop vapour diffusion method, mixing of equal volumes of protein and reservoir solutions, the latter containing 0.1 M bis-Tris. pH 5.5, 0.2 M lithium sulfate monohydrate, and 25% w/v PEG 3350, a few weeks at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
enzyme in complex with inhibitors DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, 2-(5-carbamimidamido-2-chlorophenyl)-3-sulfanylpropanoic acid, (2R)-2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid, or 5-carbamimidamido-2-(sulfanylmethyl)pentanoic acid, hanging drop vapour diffusion method, 0.21 mg/ml protein in 10 mM Tris, pH 7.0, 1 mM inhibitor, and 50 mM NaCl, mixed with an equal volume of 0.002 ml of reservoir solution containing 0.15-0.30 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, and 12-22% PEG 8000, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
crystal structures of selenium-, sulfur-, and phosphinic acid containing inhibitors bound to porcine pancreatic carboxypeptidase B are determined at 1.7, 2.15 and 1.9 A, respectively
crystals of porcine pancreatic carboxypeptidase B are grown by the capillary counter-diffusion method in the presence of polyethylene glycol and zinc acetate. The three-dimensional structure of carboxypeptidase B is determined at 1.40 A resolution. The structure contains five zinc atoms, two of which are present in the active site of the enzyme, and an acetate ion
crystals of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine are grown in a capillary in microgravity using the counter-diffusion technique. Crystals are grown in a form belonging to the same space group, P4(1)2(1)2, as the uncomplexed enzyme. X-ray data are collected to a resolution of 1.25 A
structure of the complex of the enzyme with a transition state analog N-sulfamoyl-L-phenylalanine solved at 1.74 A. Crystals of the enzyme/N-sulfamoyl-L-phenylalanine complex are grown in a capillary in microgravity using the counter-diffusion technique