Extended Data Fig. 9: The α-keto acids coupling reactions catalyzed by BbmA and the mutants BbmAG484F, and sequence alignments of HKASs revealing the key residue for acyl acceptor selectivity. | Nature Chemistry

Extended Data Fig. 9: The α-keto acids coupling reactions catalyzed by BbmA and the mutants BbmAG484F, and sequence alignments of HKASs revealing the key residue for acyl acceptor selectivity.

From: Structural insights into two thiamine diphosphate-dependent enzymes and their synthetic applications in carbon–carbon linkage reactions

Extended Data Fig. 9

a, LC-HRESIMS analysis of coupling reactions between IPA (S2) and individual aliphatic α-keto acids (S1, S4, or S12-S17) by BbmA and BbmAG484F. b, The key residues (highlighted with a red square) of known HKASs corresponding to G484 in BbmA by multiple sequence alignments.

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