Chymotrypsin: Difference between revisions
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[[Chymotrypsin]] (Chy or α-Chy) is a digestive enzyme containing an active serine residue. It cleaves peptide bonds of proteins where the amide side of the bond is an aromatic amino acid like tyrosine, phenylalanine or tryptophane. The Chy precursor is the inactive '''chymotrypsinogen''' (Chygen) which gets cleaved 4 times by trypsine losing a 6 amino | [[Chymotrypsin]] (Chy or α-Chy) is a digestive enzyme containing an active serine residue. It cleaves peptide bonds of proteins where the amide side of the bond is an aromatic amino acid like tyrosine, phenylalanine or tryptophane. The Chy precursor is the inactive '''chymotrypsinogen''' (Chygen) which gets cleaved 4 times by trypsine losing a 6 amino | ||
acid long peptide to become the active Chy. '''γ-Chy''' is a covalent acyl adduct of '''α-Chy'''. '''δ-Chy''' results when Chygen is cleaved only twice by trypsin. The images at the left and at the right correspond to one representative Chymotrypsin, ''i.e.'' the crystal structure of ''Cellulomonas Bogoriensis'' Chymotrypsin ([[2ea3]]). Some additional details in | acid long peptide to become the active Chy. '''γ-Chy''' is a covalent acyl adduct of '''α-Chy'''. '''δ-Chy''' results when Chygen is cleaved only twice by trypsin. The images at the left and at the right correspond to one representative Chymotrypsin, ''i.e.'' the crystal structure of ''Cellulomonas Bogoriensis'' Chymotrypsin ([[2ea3]]). Some additional details in<br /> | ||
*[[Molecular Playground/Chymotrypsin]]<br /> | |||
*[[Serine Proteases]]. | |||
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