Fig. 6: Molecular basis of EndoE GH18 and GH20 domains substrate specificity as visualized by LC/MS. | Nature Communications

Fig. 6: Molecular basis of EndoE GH18 and GH20 domains substrate specificity as visualized by LC/MS.

From: Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE

Fig. 6

Processing of HM-type N-glycans on RNAse B. Mass spectrometry of RNAse B treated with a no enzyme (negative control) b EndoE-GH18L c EndoE-GH18LE186Q d EndoE-GH18L + EndoE-GH18LE186Q e EndoE-GH20 f EndoE-GH20E662Q g EndoE-GH20 + EndoE-GH20E662Q h EndoBT-3987 (positive control) i EndoE j EndoE-GH18L + EndoE-GH20 k EndoEE186Q l EndoEE186Q + EndoE-GH18L m EndoEE662Q n EndoEE662Q + EndoE-GH20. The peaks corresponding to intact RNaseB are numbered based on the glycoforms found in the single glycosylation site of the protein. The retention time for RNAseB was 2.1 min. For mass deconvolution, the following parameters were used in the BioConfirm software; 1000–2400 m/z and 130–160 kDa. The theoretical and observed mass of each annotated peak are in Supplementary Table 4.

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