Fig. 5: SLG-induced d-lactylation is catalyzed by its adjacent cysteine. | Cell Research

Fig. 5: SLG-induced d-lactylation is catalyzed by its adjacent cysteine.

From: Nonenzymatic lysine d-lactylation induced by glyoxalase II substrate SLG dampens inflammatory immune responses

Fig. 5

a Motif analysis of peptide sequences around lacK sites identified in macrophages. b Nucleophilic substitutions between SLG and lysine were catalyzed by an adjacent cysteine residue. c Immunoblot of KD-La level in BMDM lysates pretreated with DTT (5 mM) or IAM (10 mM), then co-incubated with the indicated concentration of SLG. d Sequence of synthesized WT or mutated IFIT3156-166 peptide and their presumed reaction mechanism with SLG. e LC–MS detection of peptide lactylation (left) and LC–MS/MS detection of lactylation sites (right) on WT or mutated IFIT3156-166 peptides pretreated with IAM (10 mM) or not followed by SLG (1 mM) co-incubation. f Distance between different lysine (K) ε-amine groups and the spatially closest cysteine (C) β-thiol in these 3D protein structures (KC distance) calculated using Python. g 3D structure of STAT1 (PDB 1YVL) and the distance from K193 to its nearest cysteine C174. h KC distance of lacK sites we identified with different subcellular localizations.

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