Literature summary for 2.3.1.30 extracted from

Kumar, S.; Kumar, N.; Alam, N.; Gourinath, S.
Crystal structure of serine acetyl transferase from Brucella abortus and its complex with coenzyme A (2014), Biochim. Biophys. Acta, 1844, 1741-1748.

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression	Brucella abortus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme in apo state and in complex with coenzyme A, hanging drop vapour diffusion methd, mixing of 14 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5% glycerol, and 5 mM 2-mercaptoethanol with reservoir solution containing 7% w/v PEG 1000, 7% w/v PEG 3350, 5% v/v MPD, 0.12 methylene glycol, 0.1 M Tris-HCl, pH 7.4, and 50 mM MgCl2, 16°C, X-ray diffraction structure determination and analysis at 1.96 A and 1.87 A resolution, respectively	Brucella abortus

Crystallization (Comment)

Organism

purified recombinant enzyme in apo state and in complex with coenzyme A, hanging drop vapour diffusion methd, mixing of 14 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5% glycerol, and 5 mM 2-mercaptoethanol with reservoir solution containing 7% w/v PEG 1000, 7% w/v PEG 3350, 5% v/v MPD, 0.12 methylene glycol, 0.1 M Tris-HCl, pH 7.4, and 50 mM MgCl2, 16°C, X-ray diffraction structure determination and analysis at 1.96 A and 1.87 A resolution, respectively

Brucella abortus

Inhibitors

Inhibitors	Comment	Organism	Structure
L-cysteine	competitive inhibition versus L-serine, noncompetitive inhibition versus acetyl-CoA	Brucella abortus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	Michaelis-Menten kinetics, overview	Brucella abortus
0.1275	-	L-serine	recombinant enzyme, pH 8.0, temperature not specified in the publication	Brucella abortus
0.1923	-	L-serine	recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 5 mM L-cysteine	Brucella abortus
0.2783	-	L-serine	recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine	Brucella abortus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
83000	-	trimeric enzyme, gel filtration	Brucella abortus
181000	-	hexameric enzyme, gel filtration and dynamic light scattering	Brucella abortus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + L-serine	Brucella abortus	-	CoA + O-acetyl-L-serine	-	?
acetyl-CoA + L-serine	Brucella abortus 2308 A	-	CoA + O-acetyl-L-serine	-	?

Organism

Organism	UniProt	Comment	Textmining
Brucella abortus	C4IRW0	gene CysE	-
Brucella abortus 2308 A	C4IRW0	gene CysE	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme by nickel affinity chromatography and gel filtration	Brucella abortus

Reaction

Reaction	Comment	Organism	Reaction ID
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine	there is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism	Brucella abortus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acetyl-CoA + L-serine	-	Brucella abortus	CoA + O-acetyl-L-serine	-	?
acetyl-CoA + L-serine	-	Brucella abortus 2308 A	CoA + O-acetyl-L-serine	-	?
additional information	coenzyme A binds to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism	Brucella abortus	?	-	?
additional information	coenzyme A binds to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism	Brucella abortus 2308 A	?	-	?

Subunits

Subunits	Comment	Organism
hexamer	in dynamic light scattering and in crystal structure	Brucella abortus
trimer	trimer in gel filtration	Brucella abortus

Synonyms

Synonyms	Comment	Organism
SAT	-	Brucella abortus
serine acetyltransferase	-	Brucella abortus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Brucella abortus