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  • Covalent Catalysis200723

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    Anagha Chaturvedhi
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    Chymotrypsin is an enzyme synthesized and secreted by the mammalian pancreas as chymotrypsinogen, which is formed into the active enzyme through cleavage of peptide bonds. The active enzyme consists of three polypeptide chains and catalyzes the cleavage of peptide bonds on the carboxyl side of aromatic amino acids like phenylalanine, tyrosine, and tryptophan. It utilizes a catalytic triad of serine 195, histidine 57, and a water molecule to form a tetrahedral intermediate that decomposes into an acyl-enzyme intermediate and cleaves the scissile peptide bond.

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    Chymotrypsin is an enzyme synthesized and secreted by the mammalian pancreas as chymotrypsinogen, which is formed into the active enzyme through cleavage of peptide bonds. The active enzyme consists of three polypeptide chains and catalyzes the cleavage of peptide bonds on the carboxyl side of aromatic amino acids like phenylalanine, tyrosine, and tryptophan. It utilizes a catalytic triad of serine 195, histidine 57, and a water molecule to form a tetrahedral intermediate that decomposes into an acyl-enzyme intermediate and cleaves the scissile peptide bond.

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    5 views4 pages

    Covalent Catalysis200723

    Uploaded by

    Anagha Chaturvedhi
    Chymotrypsin is an enzyme synthesized and secreted by the mammalian pancreas as chymotrypsinogen, which is formed into the active enzyme through cleavage of peptide bonds. The active enzyme consists of three polypeptide chains and catalyzes the cleavage of peptide bonds on the carboxyl side of aromatic amino acids like phenylalanine, tyrosine, and tryptophan. It utilizes a catalytic triad of serine 195, histidine 57, and a water molecule to form a tetrahedral intermediate that decomposes into an acyl-enzyme intermediate and cleaves the scissile peptide bond.

    Copyright:

    © All Rights Reserved
    Download as PPTX, PDF, TXT or read online from Scribd
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    of 4

    Covalent catalysis

    Chymotrypsin
    • Synthesized and secreted as chymotrypsinogen by mammalian
    pancreas
    • Formed by the cleavage of several peptide bonds in monomeric
    chymotrypsinogen.
    • Active enzymeconsists of three nonidentical polypeptide chains
    • Chymotrypsin catalyses the cleavage of peptide bonds at the carboxyl
    side of aromatic amino acid (phenylalanine, tyrosine or tryptophan)
    residues
    Ser 195 His 57 Water as
    • Nucleop • The
    (proton • Nucleop
    nucleophil
    hilically tetrahed
    donor) e hilic
    attacks ral attack by
    the intermed water
    scissile iate molecule
    peptide’s decomp on the
    carbonyl oses to acyl–
    group to the acyl– enzyme
    form a enzyme intermed

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