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Information on EC 2.5.1.140 - N-(2-amino-2-carboxyethyl)-L-glutamate synthase and Organism(s) Staphylococcus aureus and UniProt Accession Q2G1N3

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IUBMB Comments
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
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Staphylococcus aureus
UNIPROT: Q2G1N3
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ACEGA synthase, SbnA, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACEGA synthase
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-
-
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SYSTEMATIC NAME
IUBMB Comments
O-phospho-L-serine:L-glutamate N-(2S)-2-amino-2-carboxyethyltransferase
The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-phospho-L-serine + L-glutamate
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
show the reaction diagram
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-
-
?
O-phospho-L-serine + L-glutamate
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-phospho-L-serine + L-glutamate
N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-cysteine
competitive, forms a nonproductive external aldimine with the pyridoxal 5'-phosphate cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2 - 7.1
L-glutamate
0.072 - 0.22
O-phospho-L-serine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 3.6
L-glutamate
1.6 - 2.3
O-phospho-L-serine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 1.1
L-glutamate
7.3 - 32
O-phospho-L-serine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
during staphyloferrin B 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 (ACEGA). SbnB uses NAD+ to oxidatively hydrolyze ACEGA to yield alphaoglutarate and L-2,3-diamnopropionic acid. SbnA and SbnB contribute to the iron sparing response of Staphylococcus aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in presence of O-phospho-L-serine. Formation of the pyridoxal phosphate-alpha-aminoacrylate intermediate induces closure of the active site pocket by narrowing the channel leading to the active site and forming a second substrate binding pocket that likely binds L-glutamate. Active site residues Arg132, Tyr152, Ser185 are essential for O-phospho-L-serine recognition and turnover. Mutations Y152F/S185G induce a closed form of the enzyme in the absence of the alpha-aminoacrylate intermediate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R132A
no detectable activity
S185G
about 25% of wild-type activity
Y152F/S185G
completely inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kobylarz, M.J.; Grigg, J.C.; Liu, Y.; Lee, M.S.; Heinrichs, D.E.; Murphy, M.E.
Deciphering the substrate specificity of SbnA, the enzyme catalyzing the first step in staphyloferrin B biosynthesis
Biochemistry
55
927-939
2016
Staphylococcus aureus (A6QDA0), Staphylococcus aureus Newman (A6QDA0)
Manually annotated by BRENDA team
Beasley, F.C.; Cheung, J.; Heinrichs, D.E.
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus
BMC Microbiol.
11
199
2011
Staphylococcus aureus (Q2G1N3), Staphylococcus aureus NCTC 8325 (Q2G1N3)
Manually annotated by BRENDA team
Kobylarz, M.J.; Grigg, J.C.; Takayama, S.J.; Rai, D.K.; Heinrichs, D.E.; Murphy, M.E.
Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor
Chem. Biol.
21
379-388
2014
Staphylococcus aureus (A6QDA0), Staphylococcus aureus Newman (A6QDA0)
Manually annotated by BRENDA team