Structures of α-galactosaminidases from the CAZy GH114 family and homologs defining a new GH191 family of glycosidases

Roth, C.; Moroz, O.V.; Miranda, S.A.D.; Jahn, L.; Blagova, E.V.; Lebedev, A.A.; Segura, D.R.; Stringer, M.A.; Friis, E.P.; Franco Cairo, J.P.L.; Davies, G.J.; Wilson, K.S.

doi:10.1107/S2059798325002864

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Activity measurements. The Pel substrate was mixed with different concentrations of the enzyme. The mixtures were incubated at 30°C for 30 min with shaking at 750 rev min⁻¹. The bottom (green) panel corresponds to substrate with no enzyme added, the red panel has 10 nM enzyme added and the blue panel has 50 nM enzyme added. The figure demonstrates the activity of Env-GH191 towards α-1,4-poly(N-acetyl)galactosamine. The peaks correspond to different oligomerization states of the Pel substrate. Peaks with different degrees of polymerization (DP) are indicated, with DP4 corresponding to galactoseaminetetraose (sodiated; therefore Na⁺ is shown, but only for the first peak), DP5 to galactoseaminepentaose and so on. The MS fingerprint shows weight losses of ∼160 Da, corresponding to a galactosamine monomer.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 81| Part 5| May 2025|

https://doi.org/10.1107/S2059798325002864

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