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. Author manuscript; available in PMC: 2020 Feb 1.
Published in final edited form as: Chembiochem. 2018 Nov 12;20(3):312–318. doi: 10.1002/cbic.201800481

Figure 4.

Figure 4.

Engineered OGA to enrich substrates and binding partners. A) Catalytically impaired bacterial OGA (CpOGAD298N) binds to substrate without quickly hydrolyzing the sugar. The interacting substrates can then be enriched by affinity purification of CpOGAD298N and identified by LC-MS/MS. B) The expression of an OGA-BirA fusion protein in cells results in proximity-dependent biotinylation of OGA-bound proteins, including OGA substrates. The enriched biotinylated proteins can then be detected by LC-MS/MS.