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

EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
show the reaction diagram
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
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and 81000, dynamic and multi-angle light scattering
81000
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and 71000, dynamic and multi-angle light scattering
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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