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Figure 1 | Biotechnology for Biofuels

Figure 1

From: Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability

Figure 1

Multiple alignment of amino acid sequences of the nine PODs from the P. ostreatus genome (current JGI references, after manual annotation, included). Conserved catalytic and other relevant residues are indicated with different colors including: eight cysteines (cyan) forming four disulfide bridges; nine ligands (green) of two structural Ca2+ ions; two active site histidines (dark gray); three acidic residues (orange) forming the Mn2+ oxidation site; one tryptophan (blue) responsible for aromatic substrate oxidation by VPs (also present in MnP1, initially classified as a VP); several active site conserved residues (light gray); and several lysine (purple) and proline (yellow) residues being particularly frequent in some of the sequences. Alignment was prepared using ClustalW2 (European Bioinformatics Institute, Hinxton, UK). Amino acid numbering starts at the first residue of the mature protein (red asterisk on the alignment). Symbols below indicate full conservation of the same (*) or equivalent residues (:) and partial residue conservation (.). JGI, Joint Genome Institute; MnP, manganese peroxidase; POD, class II peroxidase from the superfamily of non-animal (plant-fungal-prokaryotic) peroxidases; VP, versatile peroxidase.

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