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2.5.1.140 |
Description |
N-(2-amino-2-carboxyethyl)-L-glutamate synthase |
Alternative names |
SbnA;
ACEGA synthase;
O-phosphoserine(amino)-lyase;
L-2,3-diaminopropionate synthase, protein A |
Catalyzed reaction |
O-phospho-L-serine + L-glutamate = N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate |
Cofactor |
Pyridoxal phosphate. |
Comments |
the enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. |
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SbnA uses O-phospho-L-serine and L-glutamate to produce the unusual metabolite N-(2-amino-2-carboxyethyl)-L-glutamate (ACEGA), which in turn is oxidatively hydrolyzed by a second protein (SbnB) to yield α-ketoglutarate and L-2,3-diaminopropionic acid. In Staphylococcus aureus, the SbnA reaction is the first in the synthesis of the siderophore staphyloferrin B. |
PDB |
5D84; 5D85; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.5.1.140
BRENDA (activities) 2.5.1.140
KEGG (pathways) 2.5.1.140
PLPMDB (PLP mutants) 2.5.1.140
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References |
Kobylarz MJ, Grigg JC, Liu Y, Lee MS, Heinrichs DE, Murphy ME (2016) Deciphering the Substrate Specificity of SbnA, the Enzyme Catalyzing the First Step in Staphyloferrin B Biosynthesis Biochemistry 55 927-39. Kobylarz MJ, Grigg JC, Takayama SJ, Rai DK, Heinrichs DE, Murphy M.E. (2014) Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor Chem Biol. 21 379-88. Articles on 2.5.1.140 |
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last changed |
2018/03/19 13:22 |
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