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Literature summary for 3.4.21.62 extracted from

  • Petrillo, T.; ODonohoe, C.A.; Howe, N.; Malthouse, J.P.
    Importance of tetrahedral intermediate formation in the catalytic mechanism of the serine proteases chymotrypsin and subtilisin (2012), Biochemistry, 51, 6164-6170.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
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Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides importance of tetrahedral intermediate formation in the catalytic mechanism of the serine protease subtilisin. Substrate binding induces the formation of a strong hydrogen bond or low-barrier hydrogen bond between histidine-57 and aspartate-102 that increases the pK(a) of the active site histidine, allowing it to be an effective general base catalyst for the formation of the tetrahedral intermediate and increasing the effective molarity of the catalytic hydroxyl group of serine-195, catalytic mechanism, overview Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
subtilisin Carlsberg
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Bacillus sp. (in: Bacteria)