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Information on EC 1.5.1.51 - N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
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The expected taxonomic range for this enzyme is: Staphylococcus aureus
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EC NUMBER 
COMMENTARY 
1.5.1.51
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RECOMMENDED NAME
GeneOntology No.
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming)
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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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
physiological function
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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
physiological function
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
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2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
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2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.51)
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