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Fig. 4 | AMB Express

Fig. 4

From: Identification of the nucleophile catalytic residue of GH51 α-l-arabinofuranosidase from Pleurotus ostreatus

Fig. 4

Sequence alignment of 10 GH51 sequences. Close up on sequence alignment with 4 sequences homologous to Pleurotus ostreatus namely, Leucoagaricus gongylophorus, Meripilus giganteus, Aspergillus niger, Leucoagaricus gongylophorus, and 5 bacterial GH51 sequences from characterized enzymes Thermotoga maritima (Tm-Afase), Bacillus subtilis, Geobacillus stearohermophilus, Thermobacillus xylanilyticus (Tx-Abf), Cellvibrio japonicus. The conserved general acid residue, corresponding to Glu172 in Tm-Afase and Glu176 in Tx-Abf, is conserved in Pleurotus ostreatus sequence and its homologs, and lies in position 371 (shown encased in green with a green dot). On the alignment we show the Glu nucleophile conserved in Pleurotus ostreatus and its homologs but not in the bacterial GH51 enzymes. The Glu nucleophile lies in position 449 and is shown encased in green with a green dot. The Glu nucleophile conserved among the GH51 enzyme sequences corresponding to E281 from Tm-AFase and E298 from Tx-Abf is shown encased in orange with an orange dot, and does not align with the conserved Glu nucleophile of Pleurotus ostreatus

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