Literature summary for 2.5.1.140 extracted from

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 (2016), Biochemistry, 55, 927-939.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Staphylococcus aureus

Crystallization (Comment)

Organism

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

Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
R132A	no detectable activity	Staphylococcus aureus
S185G	about 25% of wild-type activity	Staphylococcus aureus
Y152F/S185G	completely inactive	Staphylococcus aureus

Inhibitors

Inhibitors	Comment	Organism	Structure
L-cysteine	competitive, forms a nonproductive external aldimine with the pyridoxal 5'-phosphate cofactor	Staphylococcus aureus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.072	-	O-phospho-L-serine	wild-type, pH 8.0, 22°C	Staphylococcus aureus
0.22	-	O-phospho-L-serine	mutant S185G, pH 8.0, 22°C	Staphylococcus aureus
3.2	-	L-glutamate	wild-type, pH 8.0, 22°C	Staphylococcus aureus
7.1	-	L-glutamate	mutant S185G, pH 8.0, 22°C	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	A6QDA0	-	-
Staphylococcus aureus Newman	A6QDA0	-	-

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 Newman	N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
SbnA	-	Staphylococcus aureus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
1.6	-	O-phospho-L-serine	mutant S185G, pH 8.0, 22°C	Staphylococcus aureus
2	-	L-glutamate	mutant S185G, pH 8.0, 22°C	Staphylococcus aureus
2.3	-	O-phospho-L-serine	wild-type, pH 8.0, 22°C	Staphylococcus aureus
3.6	-	L-glutamate	wild-type, pH 8.0, 22°C	Staphylococcus aureus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Staphylococcus aureus

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Staphylococcus aureus

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
0.29	-	L-glutamate	mutant S185G, pH 8.0, 22°C	Staphylococcus aureus
1.1	-	L-glutamate	wild-type, pH 8.0, 22°C	Staphylococcus aureus
7.3	-	O-phospho-L-serine	mutant S185G, pH 8.0, 22°C	Staphylococcus aureus
32	-	O-phospho-L-serine	wild-type, pH 8.0, 22°C	Staphylococcus aureus