Table 2 The models of LMCOs from fruits compared to the X-ray structures of ascorbate oxidase from Cucurbita pepo and LMCO from fungi.

From: Identification of the laccase-like multicopper oxidase gene family of sweet cherry (Prunus avium L.) and expression analysis in six ancient Tuscan varieties

Organisms Substrates

Ao (Cucurbita pepo), LMCO (Cherry)

LMCO (Litchi), Laccase (lacquer tree)

Fungal LMCO: M. albomyces, T. trogii

2,6-dimethoxyphenol MW, 154.17

Affinity: -4.3, -4.0

Affinity: -4.7, -4.6

Affinity: -4.3, -4.2

  1. Affinity, free-energy of enzyme-substrate binding (more negative value depicts better binding); Ao, Ascorbate oxidase (green); lacquer tree, Toxicodendron vernicifluum, (yellow); cherry LMCO (red); litchi LMCO (pink); M. albomyces, Melanocarpus albomyces (ascomycete, turquoise); T. trogii, Trametes trogii (basidiomycete, blue); respective colored space-filled amino acids, surface-exposed His residue involved in substrate binding that acts as a primary electron acceptor involved in shuttling electrons from the substrates (shown in various colors) to T2 and T3 copper (white spheres) via T1 Cu (black sphere), conserved Cys and His residues (black).
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