Substrates: CmnB catalyzes the condensation reaction to generate a metabolite intermediate N-(1-amino-1-carboxyl-2-ethyl)glutamic acid (ACEGA), which undergoes NAD+-dependent oxidative hydrolysis by CmnK to generate the nonproteinogenic amino acid L-Dap Products: -
SbnA and SbnB are essential for the synthesis of staphyloferrin B. Supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants
during staphyloferrin B biosynthesis, SbnA uses pyridoxal 5'-phosphate and substrates O-phospho-L-serine and L-glutamate to produce a metabolite N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid (ACEGA). SbnB uses NAD+ to oxidatively hydrolyze ACEGA to yield alphaoglutarate and L-2,3-diamnopropionic acid. SbnA and SbnB contribute to the iron sparing response of Staphylococcus aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle
SbnA and SbnB are essential for the synthesis of staphyloferrin B. Supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants
during staphyloferrin B biosynthesis, SbnA uses pyridoxal 5'-phosphate and substrates O-phospho-L-serine and L-glutamate to produce a metabolite N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid (ACEGA). SbnB uses NAD+ to oxidatively hydrolyze ACEGA to yield alphaoglutarate and L-2,3-diamnopropionic acid. SbnA and SbnB contribute to the iron sparing response of Staphylococcus aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in presence of O-phospho-L-serine. Formation of the pyridoxal phosphate-alpha-aminoacrylate intermediate induces closure of the active site pocket by narrowing the channel leading to the active site and forming a second substrate binding pocket that likely binds L-glutamate. Active site residues Arg132, Tyr152, Ser185 are essential for O-phospho-L-serine recognition and turnover. Mutations Y152F/S185G induce a closed form of the enzyme in the absence of the alpha-aminoacrylate intermediate
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