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2.1.2.2: phosphoribosylglycinamide formyltransferase 1

This is an abbreviated version!
For detailed information about phosphoribosylglycinamide formyltransferase 1, go to the full flat file.

Word Map on EC 2.1.2.2

Reaction

10-formyltetrahydrofolate
+
N1-(5-phospho-D-ribosyl)glycinamide
=
tetrahydrofolate
 +
N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide

Synonyms

2-amino-N-ribosylacetamide 5'-phosphate (glycinamide ribotide) transformylase, 2-amino-N-ribosylacetamide 5'-phosphate transformylase, 5'-phosphoribosylglycinamide transformylase, 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase, ADE8, GAR formyltransferase, GAR synthetase, GAR TFase, GAR transformylase, GARFT, GARFTase, GART, GART synthetase, GARTfase, glycinamide ribonucleotide formyl transferase, glycinamide ribonucleotide formyltransferase, glycinamide ribonucleotide transformylase, glycinamide ribotide formyltransferase, N10-formyltetrahydrolate:2-amino-N-ribosylacetamide-5'-phosphate transformylase, phosphoribosylglycinamide formyltransferase, PurN, purN transformylase, trifunctional purine biosynthetic protein adenosine-3

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.2 Hydroxymethyl-, formyl- and related transferases
                2.1.2.2 phosphoribosylglycinamide formyltransferase 1

Crystallization

Crystallization on EC 2.1.2.2 - phosphoribosylglycinamide formyltransferase 1

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 2.5 A, space group P3121
crystals grown at 20°C by hanging-drop vapor diffusion, space group C222, a = 140.9 A, b = 97.6 A, c = 102.4
-
crystals grown by vapor diffusion, space group C222, a = 140.5 A, b = 98.2 A, c = 103.3 A
-
orthorhombic space group C222, a = 141.4 A, b = 98.2 A, c = 103.5 A
-
purified recombinant enzyme in apoform or in complex with inhibitors 10S methylthio-DDACTHF and 10R methylthio-DDACTHF, mixing of 0.002 ml of 15 mg/mL in 20 mM Tris, pH 8.0, 200 mM NaCl, 5 mM DTT, and inhibitors in a 5fold molar excess for complex crystals, with 0.002 ml of reservoir solution containing 0.1 M phosphate/citrate buffer, 1.5-2.0 M ammonium sulfate at pH 4.2, X-ray diffraction structure determination and analysis at 1.52-1.70 A resolution, molecular replacement
sitting drop vapor diffusion method, using 0.1 M Tris-HCl (pH 7.5), 0.333 M NaCl, 18% (w/v) polyethylene glycol (PEG) 4000, and a 2% (w/v) PEG 400
-
vapor diffusion sitting drop method, crystals of enzyme in complex with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
in complex with magnesium and iodide at 2.2 A resolution, and with cofactor analogue 5-methyltetrahydrofolate at 2.2 A resolution
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 22 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.2 M lithium chloride, 0.1 M sodium cacodylate trihydrate, pH 6.6, 14% PEG 3350, and equilibration against 0.2 ml of reservoir solution, 18°C, method optimization, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement
-