genes SbnA and SbnB are essential for the synthesis of staphyloferrin B, and supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants
SbnA and SbnB are encoded by the staphyloferrin B biosynthetic gene cluster and are implicated in L-2,3-diaminopropionate 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. SbnB uses NAD+ to oxidatively hydrolyze N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid to yield 2-oxoglutarate and L-2,3-diaminopropionate
genes SbnA and SbnB are essential for the synthesis of staphyloferrin B, and supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants
SbnA and SbnB are encoded by the staphyloferrin B biosynthetic gene cluster and are implicated in L-2,3-diaminopropionate 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. SbnB uses NAD+ to oxidatively hydrolyze N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid to yield 2-oxoglutarate and L-2,3-diaminopropionate
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NADH and N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid as well as with NAD+ and 2-oxoglutarate, to 1.85 to 2.36 A resolution. NAD+/NADH is bound at full occupancy in a preformed rigid pocket. Each SbnB monomer contains an NAD+/NADH bound at the base of the interdomain channel between the NAD binding and dimerization domains
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1.5.1.51 N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
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