Journal
CHEMISTRY & BIOLOGY
Volume 21, Issue 3, Pages 379-388Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2013.12.011
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Funding
- Canadian Institutes of Health Research [MOP-102596]
- Department of Energy (DOE) Office of Biological and Environmental Research
- National Institutes of Health (NIH), National Institute of General Medical Sciences [P41GM103393]
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L-2,3-diaminopropionic acid (L-Dap) is an amino acid that is a precursor of antibiotics and staphyloferrin B a siderophore produced by Staphylococcus aureus. SbnA and SbnB are encoded by the staphyloferrin B biosynthetic gene cluster and are implicated in L-Dap biosynthesis. We demonstrate here that SbnA uses PLP and substrates O-phospho-L-serine and L-glutamate to produce a metabolite N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid (ACEGA). SbnB is shown to use NAD(+) to oxidatively hydrolyze ACEGA to yield alpha-ketoglutarate and L-Dap. Also, we describe crystal structures of SbnB in complex with NADH and ACEGA as well as with NAD(+) and alpha-ketoglutarate to reveal the residues required for substrate binding, oxidation, and hydrolysis. SbnA and SbnB contribute to the iron sparing response of S. aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle.
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