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
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2.6.1.82
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cadaverine
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synthesis
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l-lysine
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gamma-aminobutyric
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gamma-aminobutyraldehyde
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agmatine
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transamination
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glutamicum
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volumetric
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corynebacterium
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5-aminovalerate
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pyrroline
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putida
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adaptor
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aminotransferases
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synchrotron
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l-arginine
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clpap
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n-degron
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catabolite
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klebsiella
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l-ornithine
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polyamide
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semialdehyde
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diamines
- 2.6.1.82
- cadaverine
- synthesis
- l-lysine
-
gamma-aminobutyric
- gamma-aminobutyraldehyde
- agmatine
-
transamination
- glutamicum
-
volumetric
-
corynebacterium
- 5-aminovalerate
-
pyrroline
- putida
- adaptor
- aminotransferases
-
synchrotron
- l-arginine
- clpap
-
n-degron
-
catabolite
-
klebsiella
- l-ornithine
- polyamide
- semialdehyde
-
diamines
Reaction
Synonyms
FG99_07980, KES24511, PatA, PATase, Pp-SpuC, putrescine aminotransferase, putrescine transaminase, putrescine-alpha-ketoglutarate transaminase, putrescine:2-oxoglutarate aminotransferase, SpuC, YgjG, YjgG
ECTree
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Crystallization
Crystallization on EC 2.6.1.82 - putrescine-2-oxoglutarate transaminase
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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
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
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