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IntroductionIntroduction

is a metalloexopeptidase that hydrolytically cleaves peptides at the C-terminal peptide bond containing hydrophobic side chains Specifically, CPA is a Zn²⁺ metalloenzyme that carries out the hydrolysis of C-terminal polypeptide residues through the deprotonation of a water molecule that is coordinated to the Zn²⁺ ion in the enzyme's active site. From bovine pancreas, CPA has been crystallized in a new environment alongside two Zn²⁺ ions, one catalytic, the other inhibitory. The inhibitory Zn²⁺ ion in this more recent crystal structure not only prevents 1CPX from undergoing its hydrolysis mechanism (BLUE LINK), but also this crystallographic data reveals a different conformation of the Tyr248 (GREEN LINK) residue suggesting alternative mechanistic behavior (CITE). 1CPX consists of a single polypeptide chain that contains 307 amino acids. Produced in bovine pancreas, CPA itself must first be activated by either trypsin or chymotrypsin in order to achieve an active form that serves its biological function.. This crystallographic data presents 1CPX activated by trypsin in its β-form and orthorhombic crystal form.

This is about 1CPX. This is a carboxypeptidase from bovine pancreas with two Zinc binding sites.This is about 1CPX. This is a carboxypeptidase from bovine pancreas with two Zinc binding sites.This is about 1CPX. This is a carboxypeptidase from bovine pancreas with two Zinc binding sites.This is about 1CPX. This is a carboxypeptidase from bovine pancreas with two Zinc binding sites.This is about 1CPX.

This is a carboxypeptidase from bovine pancreas with two Zinc binding sites.

spinqualitylabelsall models This is a caption about 1CPX Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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