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Literature summary for 2.5.1.140 extracted from

  • Beasley, F.C.; Cheung, J.; Heinrichs, D.E.
    Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus (2011), BMC Microbiol., 11, 199.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O-phospho-L-serine + L-glutamate Staphylococcus aureus
-
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
-
?
O-phospho-L-serine + L-glutamate Staphylococcus aureus NCTC 8325
-
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q2G1N3
-
-
Staphylococcus aureus NCTC 8325 Q2G1N3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-L-serine + L-glutamate
-
Staphylococcus aureus N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
-
?
O-phospho-L-serine + L-glutamate
-
Staphylococcus aureus NCTC 8325 N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
-
?

Synonyms

Synonyms Comment Organism
SbnA
-
Staphylococcus aureus

General Information

General Information Comment Organism
physiological function SbnA and SbnB are essential for the synthesis of staphyloferrin B. Supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants Staphylococcus aureus