PDB Code: 3FU8
UniProt Code: Q70KY3
Base Pairs: 1677
Origin: Melanocarpus albomyces
Usage and Biology
Laccases (p-diphenol:dioxygen oxidoreductases; EC 126.96.36.199) are widely distributed in nature. These enzymes can be found in almost all known fungal organisms and in many plants, insects and bacteria.
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.
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.
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21Illegal BglII site found at 1030
Illegal BglII site found at 1333
- 23COMPATIBLE WITH RFC
- 25COMPATIBLE WITH RFC
- 1000Illegal BsaI.rc site found at 1059
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.