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PPT-1
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Inhibitors of PPT-1PPT-1 is a lysosomal enzyme which had a serine lipase consensus sequence; a key characteristic of lysosomal enzymes. Despite having a serine lipase consensus sequence, PPT-1, is not deactivated by phenylmethylsulfonyl fluoride (PMSF), a common serine-modifying reagent. Hexadecylsulfonylfluoride (HDSF) is a serine-modifying reagent that is able to inhibit the actions of PPT1 by binding to PPT-1. Unlike other inhibitors, HDSF is able to fit in the narrow, hydrophobic groove of PPT-1 leading away from the active site of PPT-1. PMSF is unable to fit into this small narrow groove due to steric constraints that relate to the unique structure of the substrate-binding site of PPT1. The sulphur of HDSF will bind to SER-115 in the active site of PPT-1 via a sulponylation reaction and thus will inhibit the actions of PPT-1.
HDSF is able to fit in the narrow, hydrophobic groove of PPT-1 binds to SER-115 in the active site of PPT-1 bind to SER-115 in the active site of PPT-1
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