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2.3.1.57: diamine N-acetyltransferase

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

Word Map on EC 2.3.1.57

Reaction

acetyl-CoA
+
an alkane-alpha,omega-diamine
=
CoA
 +
an N-acetyldiamine

Synonyms

acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase, acetyltransferase, putrescine, bltD, CpSSAT, diamine acetyltransferase, More, N1-SAT, N1-spermidine/spermine acetyltransferase, N1SSAT, PaiA, putrescine (diamine)-acetylating enzyme, putrescine acetylase, putrescine acetyltransferase, putrescine N-acetyltransferase, SAT, SAT1, SpeG, spermidine /spermine N1-acetyltransferase, spermidine acetyltransferase, spermidine N-acetyltransferase, spermidine N1-acetyltransferase, spermidine-spermine acetyltransferase, spermidine-spermine N1-acetyltransferase, spermidine/spermine acetyltransferase, spermidine/spermine N-acetyltransferase, spermidine/spermine N1-acetyltransferase, spermidine/spermine N1-acetyltransferase 1, spermidine/spermine N1-acetyltransferase 2, spermidine/spermine N1-acetyltransferase-1, spermidine/spermine-N 1-acetyltransferase, spermidine/spermine-N1-acetyltransferase, spermidine/spermine-N1-acetyltransferase activity, SSAT, SSAT-1, SSAT-2, SSAT1, SSAT2, SSATX, Ste27, Ta0374, VCA0947

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.57 diamine N-acetyltransferase

Crystallization

Crystallization on EC 2.3.1.57 - diamine N-acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of PaiA in complex with CoA at 1.9A resolution, crystals belong to space group C222(1), with cell parameters of alpha = 39.9 A, beta = 135.8 A and gamma = 132.4 A
-
in complex with spermidine and CoA, sitting drop vapor diffusion method, using 0.1 M Ca-acetate, 0.05 M Na-cacodylate pH 6.5, and 9% (w/v) PEG8000
purified recombinant enzyme, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 40 mg/ml protein in 10 mM HEPES-KOH pH 7.5, 50 mM CoA, 50 mM spermidine, 300 mM KCl, 0.1 mM EDTA, 6 mM 2-mercaptoethanol, 10% glycerol, 10 mM PMSF, 0.02% Brij-35, with 0.001 ml of reservoir solution containing 50 mM sodium cacodylate, pH 6.5, 9% w/v PEG 8000, 0.1 M calcium acetate, and equilibration against 0.5 ml reservoir solution, 20°C, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
sitting drop vapor diffusion method, using 0.2 M ammonium phosphate monobasic, 0.1 M Tris, 50% (w/v) 2-methyl-2,4-pentanediol, pH 8.5
small angle X-ray scattering curves from two sets of a two-fold dilution series containing five sample dilutions of enzyme with and without presence of spermine
precipitation with polyethylene glycol, high resolution structures of wild-type and mutant SSAT, as the free dimer and in binary and ternary complexes with CoA, acetyl-CoA, spermine, and the inhibitor N1,N11-bis-(ethyl)-norspermine
-
SSAT bound to a bisubstrate analogue N1-spermine-acetyl-CoA
-
three-dimensional crystal structure of SSAT with bound bisubstrate inhibitor, solved at 2.3 A resolution, hanging drop method, data and refinement statistics
SSAT in complex with coenzyme A, with and without bound spermine, hanging drop vapor diffusion method at 4°C, crystals of the binary complex between SSAT and CoA are obtained in 20% PEG 8000, 80 mM sodium acetate, 15% glycerol, 2 mM spermine, 1 mM CoA, and 85 mM sodium cacodylate, pH 6.0, 0.001 ml of the protein solution is mixed with 0.01 ml of precipitant solution containing 20% PEG 8000, 50 mM NaCl, 2 mM spermine, 1 mM coenzyme A, 15% glycerol, and 100 mM bicine buffer, pH 9.0. Crystals are obtained at pH 5.0-6.5 over a broad range of precipitant and salt concentrations. Introduction of spermine results in displacement of CoA from the enzyme active site. X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution
molecular modeling of structure. Both spermidine and spermine should bind at unique position with high specificity
crystal structure is determined in an apo-form and in complex with its natural ligand (acetyl coenzyme A) and in complex with a product of reaction (coenzyme A) obtained by cocrystallization with spermidine
enzyme in ligand-free form or complxed with spermine or spermidine, and/or acetyl-CoA, X-ray diffraction structure determination and analysis at 1.85-2.83 A resolution, the enzyme occurs in open and closed conformations
purified enzyme, dodecameric structure in a ligand-free form in three different conformational states, open, intermediate and closed, sitting drop vapor diffusion method, for open state crystals: mixing of 400 nl of 10 mg/ml protein in 100 mM sodium chloride, 10 mM HEPES, pH 7.5, with 400 nl of reservoir solution containing 8% isopropanol and 0.1 M Tris-HCl, pH 8.5, for closed state crystals: mixing of 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, with 0.001 ml of reservoir solution that contains 0.05 M ammonium sulfate, 0.1 M tri-sodium citrate and 15% polyethylene glycol 8000, and for intermediate state crystals: 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, and 0.001 ml of reservoir solution containing 0.01 M calcium chloride, 20% methanol, and 0.1 M Tris-HCl, pH 8.5, 19°C, X-ray diffraction structure determination and analysis at 2.38-2.88 A reolution, molecular replacement. All structures are crystallized in C2 space group symmetry and contain six monomers in the asymmetric unit cell. Two hexamers related by crystallographic 2fold symmetry form the SpeG dodecamer. The open and intermediate states have a unique open dodecameric ring