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

BRENDA support

2.6.1.82: putrescine-2-oxoglutarate transaminase

This is an abbreviated version!
For detailed information about putrescine-2-oxoglutarate transaminase, go to the full flat file.

Word Map on EC 2.6.1.82

Reaction

4-aminobutanal
=
1-Pyrroline
 +
H2O

Synonyms

FG99_07980, KES24511, PatA, PATase, Pp-SpuC, putrescine aminotransferase, putrescine transaminase, putrescine-alpha-ketoglutarate transaminase, putrescine:2-oxoglutarate aminotransferase, SpuC, YgjG, YjgG

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.82 putrescine-2-oxoglutarate transaminase

Crystallization

Crystallization on EC 2.6.1.82 - putrescine-2-oxoglutarate transaminase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of YgjG at 2.3 and 2.1 A resolutions for the free and putrescine-bound enzymes, respectively. YgjG forms a dimer that adopts a class III pyridoxal 5'-phosphate-dependent aminotransferase fold. Structures of YgjG and other class III aminotransferases are similar. YgjG has an additional N-terminal helical structure that partially contributes to a dimeric interaction with the other subunit via a helix-helix interaction. The YgjG substrate-binding site entrance size and charge distribution are smaller and more hydrophobic than other class III aminotransferases
hanging-drop vapour-diffusion method, PEG 3350, pH 7.5
purified recombinant enzyme in apoform, sitting drop vapour diffusion method, best from 0.2 M MgCl2, 0.1 M Bis-Tris, pH 6.5, and 25% PEG 3350, at 20°C, X-ray diffraction structure determination analysis at 2.1 A resolution, molecular replacement method, structure modelling using the structure of aspartate aminotransferase from Pseudomonas sp. (PDB ID 5TI8) as the search model
purified recombinant His-tagged enzyme, sitting drop vapour diffusion metod, mixing of 150 nl of 10.5 mg/ml protein in 25 mM Tris chloride, 137 mM NaCl, and 3 mM KCl, pH 8.0, with 150 nl of reservoir solution containing 0.066 M calcium acetate, 18% w/v PEG MME 5000, 0.1 M Tris chloride, pH 7.6, and equilibration against 0.5 ml of reservoir solution, at 20°C, method optimization, X-ray diffraction structure determination analysis at 2.07 A resolution, molecular replacement method, structure modelling using the structure of a Chromobacterium violaceum omega transaminase monomer (PDB ID 4a6t) as the search model
-