Fig. 4: Modification of the HAS catalytic region for highly efficient synthesis of HA.

A Protein structure of SzHAS2P/3I/4F/6R/17L/89V/90G/96W/108H/109D/243K predicted by AlphaFold2. B–D HA production by C. glutamicum strains with mutations at residues 89-90, 96, 108-109, and 243 of SzHAS2P/3I/4F/6R/17L. Residues Q89-Q90 and E108-T109 of the variant SzHAS2P/3I/4F/6R/17L were used to construct 200 engineered mutant strains, and the mutant with the strongest HA synthesis ability was selected. E Growth, glucose consumption, and HA synthesis of C. glutamicum expressing SzHAS2P/3I/4F/6R/17L/89V/90G/96W/108H/109D/243K. All data are expressed as the mean ± S.D. from three (n = 3) independent biological replicates. Source data are provided as a Source Data file.