Total synthesis of
anguibactin was accomplished for the first time,
and the following biochemical characterizations allowed for the determination
of its Fe(III) binding mode as well as the demonstration of its iron
delivery capability for Acinetobacter baumannii. These properties, in addition to the thermal stability over acinetobactin,
render anguibactin as a competent surrogate siderophore that can be
useful for the future development of a siderophore-based antibiotic
delivery system against A. baumannii.
Succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of γ-aminobutyric acid degradation. Here, we characterized Bacillus subtilis SSADH (BsSSADH) regarding its cofactor discrimination and substrate inhibition. BsSSADH showed similar values of the catalytic efficiency (kcat/Km) in both NAD(+) and NADP(+) as cofactors, and exhibited complete uncompetitive substrate inhibition at higher SSA concentrations. Further analyses of the sequence alignment and homology modeling indicated that the residues of catalytic and cofactor-binding sites in other SSADHs were highly conserved in BsSSADH.
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