3.4.17.2: carboxypeptidase B

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

Word Map on EC 3.4.17.2

Reaction

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

Synonyms

More, TAFI, EC 3.4.2.2, EC 3.4.12.3, 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

ECTree

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

Crystallization

Crystallization on EC 3.4.17.2 - carboxypeptidase B

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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