Part:BBa_K3511000

Papain G23W

Papain is an enzyme that was first found to be effective in degrading plastic polymers in blood-contacting devices such as catheters and heart assist pumps made of polyurethane (PUR) (Phua et al., 1987). Papain is capable of catalysing enzymatic hydrolysis of urethane and urea linkages, and degrades PUR into amines and hydroxyl end products.

Papain G23W is a mutant papain created by in-silico single amino acid mutation at a PUR-binding region of papain. The glycine residue at the 23rd position in papain is changed to tryptophan to enhance the hydrophobicity of the ligand-binding site. The Gibbs free energy (ΔG) of the mutant papain G23W with PUR tetramer as ligand was shown by redocking analysis to be -8.6 kcal/mol, while the ΔG of native papain binding to PUR tetramer is -7.6 kcal/mol. Hence, papain G23W exhibited a higher binding affinity to PUR tetramer ligand than the native papain, and this change may enhance the efficiency of PUR biodegradation of the enzyme.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]