Part:BBa_K4077000

Profile

PDB Code: 3FU8
UniProt Code: Q70KY3
Base Pairs: 1677
Origin: Melanocarpus albomyces

Usage and Biology

Laccases (p-diphenol:dioxygen oxidoreductases; EC 1.10.3.2) are widely distributed in nature. These enzymes can be found in almost all known fungal organisms and in many plants, insects and bacteria.[1]
Laccases can oxidize an extensive variety of phenolics, along with other organic and even inorganic substrates using molecular oxygen as a terminal electron acceptor. M. albomyces is an ascomycete fungus producing a laccase with high thermal stability and pH optimum at a neutral pH range.[3]
MaL also has a unique C-terminal tail when compared with the other laccases and multicopper oxidases. The last four residues of the C-terminus of recombinant MaL (rMaL) penetrate into the cavity leading toward the trinuclear site.[2]

Fig: 3FU8 visualised in PyMol.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 1030
  Illegal BglII site found at 1333
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal BsaI.rc site found at 1059
  

References

1. Mayer, A. M. & Staples, R. C. (2002). Laccase: new functions for an old enzyme. Phytochemistry, 60, 551–565.
2. Hakulinen, N., Kiiskinen, L.-L., Kruus, K., Saloheimo, M., Paananen, A., Koivula, A. & Rouvinen, J. (2002). Crystal structure of a laccase from Melanocarpus albomyces with intact trinuclear copper site. Nat. Struct. Biol. 9, 601–605.
3. Kiiskinen, L.-L., Viikari, L. & Kruus, K. (2002). Purification and characterization of a novel laccase from the ascomycete Melanocarpus albomyces. Appl. Microbiol. Biotechnol. 59, 198–204.