Part:BBa_K3511001

PueA R392F

Polyurethanase esterase A (PueA) is an enzyme with an esterase activity and has a high affinity for polyurethane (PUR) (Stern & Howard, 2006). In theory, all ester bonds in PUR can be broken by the pueA enzyme (Howard, 2011).

PueA R392F is a mutant of pueA created by in-silico single amino acid mutation at the PUR binding region of pueA. The polar arginine residue at position 392 is changed to a non-polar phenylalanine residue. The Gibbs free energy (ΔG) of the mutant pueA R392F binding with a PUR tetramer ligand is -8.8 kcal/mol, while the ΔG of binding of the native pueA to PUR tetramer is -8.2 kcal/mol. The mutant pueA R392F has a higher binding affinity for PUR than the native pueA, and this change may enhance the PUR degradation efficiency 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]