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Substrate binds to the hydrophobic pocket.
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Histidine acts as a general base to active a serine OH group.
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A serine alkoxide ion attacks a carbonyl carbon of the substrate, forming a covalent acyl bond between enzyme and substrate.
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A tetrahedral transition state involving an oxyanion is stabilized by the oxyanion hole.
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Histidine acts as a general acid to protonate an amide nitrogen. The peptide bond is broken and the first product dissociates.
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Histidine acts a general base to convert water into a hydroxide ion.
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Histidine acts as a general acid to protonate the serine oxygen group, breaking the acyl bond between enzyme and substrate. The second product dissociates.
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