2.3.1.30: serine O-acetyltransferase

This is an abbreviated version!
For detailed information about serine O-acetyltransferase, go to the full flat file.

Reaction

Synonyms

acetyltransferase, serine, AtOASS, AtSAT, AtSAT1, AtSerat 2;1, BvSAT, CysE, cytosolic serine acetyltransferase, DcsE, EhSAT1, EhSAT2, EhSAT3, GmSerat2,1, HISAT, Kpn CysE, L-serine acetyltransferase, L-serine O-acetyltransferase, L-serineO-acetyltransferase, More, plastidic serine acetyltransferase, SAT, SAT isoform 1, SAT-1, SAT1, SAT2, SAT3, SATase, SERAT, Serat1,1, SERAT1.1, Serat2,1, Serat2,2, SERAT2.1, Serat3,1, Serat3,2, serine acetlytransferase, serine acetyltransferase, serine acetyltransferase 1, serine acetyltransferase 2,1, serine O-acetyltransferase, serine O-acetyltransferase 1, serine transacetylase, Spn cysE, SP_0589

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.30 serine O-acetyltransferase

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Results	in table
38479	AA Sequence
7	Application
1	CAS Registry Number
55	Cloned(Commentary)
7	Cofactor
11	Crystallization (Commentary)
6	Expression
39	General Information
22	IC50 Value
105	Inhibitors
4	kcat/KM [mM/s]
28	Ki Value [mM]
88	KM Value [mM]
55	Localization
6	Metals/Ions
40	Molecular Weight [Da]
83	Natural Substrates/ Products (Substrates)
488	Organism
14	Pathway
75	PDB ID
23	pH Optimum
2	pH Range
5	pI Value
1	Posttranslational Modification
103	Protein Variants
34	Purification (Commentary)
9	Reaction
1	Reaction Type
109	Reference
36	Source Tissue
51	Specific Activity [micromol/min/mg]
8	Storage Stability
137	Substrates and Products (Substrate)
43	Subunits
190	Synonyms
1	Systematic Name
18	Temperature Optimum [°C]
4	Temperature Range [°C]
5	Temperature Stability [°C]
14	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.30 - serine O-acetyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

vapor diffusion method. Crystal structure of Arabidopsis thaliana O-acetylserine aulfhydrylase bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase (C10 peptide) at 2.9 A resolution

Arabidopsis thaliana

-

676429

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

C4IRW0

735709

crystal structure of serine acetyltransferase (SAT) isoform 1 at 1.77 A, in complex with its substrate serine at 1.59 A and inhibitor Cys at 1.78 A resolution is reported

Entamoeba histolytica

Q9U8X2

719916

crystal structure of the enzyme with its inhibitor L-cysteine

Escherichia coli

P0A9D4

676935

hanging drop vapour diffusion method, 8-16% polyethylene glycol 1000, 10 mM Tris-HCl, pH 7.5, 2-4 weeks, room temperature, structure analysis

Escherichia coli

-

486757

recombinant enzyme, crystals grew from 0.1 M MES, pH 6.6, 1ß% 2-methyl-2,3-pentanediol, 0.5 M sodium thiocyanate, 5.5 mM cysteine, and SeMet SAT (10 mg/ml) sitting drops, at 20°C within 7 days. 2.2 A crystal structure of the enzyme, which is s dimer of trimers in complex with cysteine

Escherichia coli

P0A9D4

659391

purified enzyme in apoform and complexed with L-serine and CoA, hanging drop vapor diffusion method, mixing of 0.005 ml of 10-20 mg/ml protein in 10 mM Tris, pH 8.0, 50 mM NaCl, and 5 mM 2-mercaptoethanol with 0.005 ml of reservoir solution, containing 1.8 M ammonium phosphate, 100 mM imidazole, pH 8.0, and equilibration ver 0.5 ml reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.7-3.0 A resolution, method optimization

Glycine max

Q5MYA1

736438

crystals of Haemophilus influenzae O-acetylserine sulfhydrylase (EC 2.5.1.47) in complex with the C-terminal 10-residue peptide of serine acetyltransferase are prepared under silicon oil by using the sitting drop method

Haemophilus influenzae

-

662033

X-ray crystallographic structure of the enzyme in binary complexes with cysteine and CoA and refined to resolutions of 1.85 and 2.0 A, respectively

Haemophilus influenzae

-

671580

purified His-tagged enzyme in complex with L-cysteine, mixing of 0.002 ml of 30 mg/ml protein in 20 mM Tris pH 8.0; 50 mM NaCl and 5% glycerol, with 0.0016 ml of reservoir solution with 400 nl 3% w/v trimethylamine N-oxide dehydrate additive and 25% ethylene glycol as precipitant, and equilibration against reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement using Escherichia coli CysE hexameric structure (PDB ID 1T3D) as a search model

Klebsiella pneumoniae

Q0ZB96

756960

purified recombinant wild-type and mutant G52A-P55G enzymes, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml of protein in 20 mM Tris-HCl, pH 7.6, 0.2 M NaCl, 5 mM dithiothreitol, and 1 mM EDTA, with 0.001 ml of precipitant solution containing 0.1 M Tris-HCl, pH 7.5, 25% w/v PEG 4000, and 0.2 M ammonium acetate, 3 weeks, structure modeling, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution

Streptomyces lavendulae

D2Z028

736358