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Literature summary for 3.4.21.1 extracted from

  • Cai, J.; Rosenzweig, B.; Hamilton, A.
    Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments (2009), Chemistry, 15, 328-332.
    View publication on PubMed

Application

Application Comment Organism
drug development G-quadruplex-scaffold-based receptors are effective inhibitors of ChT by protein-surface recognition. This may provide a general strategy to generate synthetic combinatorial libraries of receptors to target different classes of proteins synthetic construct

Inhibitors

Inhibitors Comment Organism Structure
additional information efficient binding and inhibition of ChT by a self-assembled DNA quadruplex with protein recognition fragments appended on the 5'-ends of the assembled G-quartet: quadruplex containing two anionic residues in each loop (GDGD) displays the highest inhibition potency for ChT, exhibits slow binding inhibition. Quadruplex containing one anionic and one hydrophobic residue (GDGY) strongly inhibits ChT activity, exhibits slow binding inhibition. Quadruplex without tethered loops or containing a peptide loop tethered to a single strand of a sequence that is incapable of forming self-assembled structures, are weak inhibitors synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
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synthetic construct N-benzoyl-L-tyrosine + p-nitroaniline
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?

Synonyms

Synonyms Comment Organism
alpha-chymotrypsin
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synthetic construct
CHT
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synthetic construct
chymotrypsin
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synthetic construct