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Literature summary for 3.4.17.1 extracted from

  • Arolas, J.L.; Popowicz, G.M.; Bronsoms, S.; Aviles, F.X.; Huber, R.; Holak, T.A.; Ventura, S.
    Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond (2005), J. Mol. Biol., 352, 961-975.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in complex with leech carboxypeptidase inhibitor, complexing in 50 mM Tris-HCl, pH 7.5, and 100 mM NaCl, at 20°C, complex purification by gel filtration, crystallization by mixing of equal volumes of protein, containing 10-12 mg/ml protein, and reservoir solutions, the latter containing 1.5 M lithium sulfate monohydrate and 100 mM Tris, pH 8.5, sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.2 A resolution Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
leech carboxypeptidase inhibitor LCI, tight-binding, competitive inhibition, the inhibitor contains four disulfide bonds, biding structure with CPA, oxidative folding pathway and intermediate of wild-type and mutant C19A/C43A mutant, determination of thermodynamics and conformational stability of wild-type and mutant enzymes at pH 8.4/high concentration of DTT, overview Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
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Subunits

Subunits Comment Organism
More structure analysis of enzyme in complex with leech carboxypeptidase inhibitor Bos taurus

Synonyms

Synonyms Comment Organism
CPA
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Bos taurus