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. Author manuscript; available in PMC: 2020 Feb 1.
Published in final edited form as: J Mol Biol. 2018 Dec 7;431(3):524–541. doi: 10.1016/j.jmb.2018.11.030

Fig. 8.

Fig. 8.

Inactivation of LsALDH16 by DEAB. (A) Time-dependence of the loss of catalytic activity in the presence of DEAB. LsALDH16 was incubated with DEAB and NAD+, and then aliquots were taken at various time points and assayed for activity using hexanal as the substrate and NAD+ as the cofactor. (B) Mass spectrometry evidence for the covalent modification of LsALDH16 by DEAB. The observed mass shift of 175 Da is consistent with previous studies of the inactivation of ALDHs by DEAB [41, 42].