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Literature summary extracted from

  • Pearlstein, R.; Hu, Q.; Zhou, J.; Yowe, D.; Levell, J.; Dale, B.; Kaushik, V.; Daniels, D.; Hanrahan, S.; Sherman, W.; Abel, R.
    New hypotheses about the structure-function of proprotein convertase subtilisin/kexin type 9: Analysis of the epidermal growth factor-like repeat A docking site using WaterMap (2010), Proteins, 78, 2571-2586.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.61 D374Y mutant kinetic data show a slower k-off for substrate domain EGF-A and full-length low density lipoprotein receptor unbinding which stems from the destabilizing effects of this mutation on PCSK9 hydration sites, with a concomitant increase in the persistence of the bound complex Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.61 additional information
-
 additional information analysis of binding kinetics data for PCSK9 with full-length low density lipoprotein receptor ectodomain, and isolated EGF-A repeat of low density lipoprotein receptor. The fast k-on and entropically driven thermodynamics observed for PCSK9-EGF-A binding stem from the functional replacement of water occupying stable PCSK9 hydration sites. The relatively fast k-off observed for EGF-A unbinding stems from the limited displacement of solvent occupying unstable hydration sites. Conversely, the slower k-off observed for EGF-A and low density lipoprotein receptor unbinding from mutant D374Y stems from the destabilizing effects of this mutation on PCSK9 hydration sites, with a concomitant increase in the persistence of the bound complex Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.61 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.61 low density lipoprotein receptor + H2O
-
 Homo sapiens ?
-
 ?