fig4

Assimilation of arabinogalactan side chains with novel 3-<i>O</i>-β-L-arabinopyranosyl-α-L-arabinofuranosidase in <i>Bifidobacterium pseudocatenulatum</i>

Figure 4. Comparison of amino acid residues at the catalytic site among Bifidobacterium GH39s. A: Comparison of amino acid residues at the catalytic sites, according to a previous report[24]. Catalytic residues (red) and residues with variation (yellow) across GH39 sequences are presented. The phylogenetic tree depicted on the left was constructed via the neighbor-joining method based on aligned Bifidobacterium GH39 sequences. GH39 sequences were aligned using the Clustal W program via MEGA11 software; B: The predicted structures of AAfase (left) and GAfase (right) are depicted as a surface representation. AlphaFold2 (ColabFold) was used to obtain the structural model with default settings. Predicted catalytic residues are highlighted in red, and different amino acid residues (Tyr116 in AAfase and Asn119 in GAfase) are highlighted in yellow.

Microbiome Research Reports
ISSN 2771-5965 (Online)

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