| Entry |
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| Name |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase;
SbnB
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| Class |
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
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| Sysname |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming)
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| Reaction(IUBMB) |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+ [RN: R11655]
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| Reaction(KEGG) |
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| Substrate |
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate [CPD: C21559];
NAD+ [CPD: C00003];
H2O [CPD: C00001]
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| Product |
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| Comment |
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
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| History |
EC 1.5.1.51 created 2017
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| Pathway |
| ec00997 | Biosynthesis of various secondary metabolites - part 3 |
| ec01110 | Biosynthesis of secondary metabolites |
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| Orthology |
| K21721 | N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase |
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| Genes |
» show all
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| Reference |
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| Authors |
Beasley FC, Cheung J, Heinrichs DE |
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| Title |
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. |
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| Journal |
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| Reference |
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| Authors |
Kobylarz MJ, Grigg JC, Takayama SJ, Rai DK, Heinrichs DE, Murphy ME |
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| Title |
Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.5.1.51 |
| ExPASy - ENZYME nomenclature database: | 1.5.1.51 |
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| LinkDB |
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