Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.30 recombinant expression Brucella abortus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.30 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.30 additional information
-
 additional information Michaelis-Menten kinetics, overview Brucella abortus
2.3.1.30 0.1275
-
 L-serine recombinant enzyme, pH 8.0, temperature not specified in the publication Brucella abortus
2.3.1.30 0.1923
-
 L-serine recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 5 mM L-cysteine Brucella abortus
2.3.1.30 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.30 83000
-
 trimeric enzyme, gel filtration Brucella abortus
2.3.1.30 181000
-
 hexameric enzyme, gel filtration and dynamic light scattering Brucella abortus

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.30 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.30 acetyl-CoA + L-serine
-
 Brucella abortus CoA + O-acetyl-L-serine
-
 ?
2.3.1.30 acetyl-CoA + L-serine
-
 Brucella abortus 2308 A CoA + O-acetyl-L-serine
-
 ?
2.3.1.30 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 ?
-
 ?
2.3.1.30 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

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

Synonyms

EC Number Synonyms Comment Organism
2.3.1.30 SAT
-
 Brucella abortus
2.3.1.30 serine acetyltransferase
-
 Brucella abortus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.30 8
-
 assay at Brucella abortus