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[The structure of pepsin. II. Structure of the enzyme active site (at 2 angstroms resolution)].

A. E. Gushchina, Natalia S. Andreeva

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Abstract

Detailed structure of the pepsin active site in the region of the active aspartic acid residues and substrate binding S1 and S1' sites is considered. At the active site of the enzyme crystals studied several molecules of ethanol were detected, which interact with active groups. The catalytic properties of aspartyl proteinases towards dipeptide substrates were explained on the base of the specific structure of S1 and S1' binding sites.

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What this paper is about

Detailed structure of the pepsin active site in the region of the active aspartic acid residues and substrate binding S1 and S1' sites is considered. At the active site of the enzyme crystals studied several molecules of ethanol were detected, which interact with active groups. The catalytic properties of aspartyl proteinases towards dipeptide substrates were explained on the base of the specific structure of S1 and S1' binding sites.

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Available abstract

Detailed structure of the pepsin active site in the region of the active aspartic acid residues and substrate binding S1 and S1' sites is considered. At the active site of the enzyme crystals studied several molecules of ethanol were detected, which interact with active groups. The catalytic properties of aspartyl proteinases towards dipeptide substrates were explained on the base of the specific structure of S1 and S1' binding sites.

Key concepts: Active site, Chemistry, Binding site, Pepsin, Substrate (aquarium), Dipeptide, Active center, Enzyme

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[The structure of pepsin. II. Structure of the enzyme active site (at 2 angstroms resolution)]. — Research Paper | ScholarLens