Structure-function analysis of 2-sulfamoylacetic acid synthase in altemicidin biosynthesis.

Altemicidin and its analogs are valuable sulfonamide antibiotics with valuable antitumor and antibacterial activities. Structures of altemicidin and congeners feature an unusual sulfonamide side chain. In the biosynthesis of altemicidin, the aldehyde dehydrogenase SbzJ catalyzes the conversion of 2-sulfamoylacetic aldehyde into 2-sulfamoylacetic acid, a key step in producing the sulfonamide side chain.

Molecular basis for the diversification of lincosamide biosynthesis by pyridoxal phosphate-dependent enzymes.

The biosynthesis of the lincosamide antibiotics lincomycin A and celesticetin involves the pyridoxal-5'-phosphate (PLP)-dependent enzymes LmbF and CcbF, which are responsible for bifurcation of the biosynthetic pathways. Despite recognizing the same S-glycosyl-L-cysteine structure of the substrates, LmbF catalyses thiol formation through β-elimination, whereas CcbF produces S-acetaldehyde through decarboxylation-coupled oxidative deamination. The structural basis for the diversification mechanism remains largely unexplored.