- Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution.
Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution.
Nature (1986-01-02)
M N James, A R Sielecki
PMID3941737
ABSTRACT
The only well-understood mechanism of zymogen activation is that of the serine proteinases, in which proteolytic cleavage leads to conformational changes resulting in a functional active site. A different mechanism is now unveiled by the crystal structure of pepsinogen. Salt bridges that stabilize the positioning of the N-terminal proenzyme segment across the active site of pepsin are disrupted at low pH, releasing the amino-terminal segment and thereby exposing the catalytic apparatus and the substrate-binding sites.
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Pepsin−Agarose from porcine gastric mucosa, lyophilized powder, ≥30 units/mg dry solid
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Pepsin from porcine gastric mucosa, lyophilized powder, ≥2,500 units/mg protein (E1%/280)
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