Literature summary extracted from
Bonatto, A.C.; Couto, G.H.; Souza, E.M.; Araujo, L.M.; Pedrosa, F.O.; Noindorf, L.; Benelli, E.M.
Purification and characterization of the bifunctional uridylyltransferase and the signal transducing proteins GlnB and GlnK from Herbaspirillum seropedicae (2007), Protein Expr. Purif., 55, 293-299.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.7.7.59 |
2-oxoglutarate |
required compound, uridylylation assay with 5 mM 2-oxoglutarate |
Herbaspirillum seropedicae |
|
2.7.7.59 |
ATP |
required compound, uridylylation assay with 0.2 mM ATP |
Herbaspirillum seropedicae |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.7.59 |
expression in Echerichia coli RB9065lambdaDE3 |
Herbaspirillum seropedicae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.7.59 |
glutamine |
shows an inhibition of 65% of GlnB uridylylation and 70% of GlnK uridylylation |
Herbaspirillum seropedicae |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.7.59 |
K+ |
uridylylation assay with 100 mM KCl |
Herbaspirillum seropedicae |
|
2.7.7.59 |
Mg2+ |
uridylylation assay with 25 mM Mg2+ |
Herbaspirillum seropedicae |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.7.59 |
Herbaspirillum seropedicae |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.7.59 |
GlnD is less soluble than the purified PII proteins GlnB or GlnK, to improve solubility of GlnD a special buffer is utilised (50 mM Tris-HCl, pH 7.0, 200 mM NaCl, 1 mM DTT) which produces 50% solubilization |
Herbaspirillum seropedicae |
2.7.7.59 |
protein is purified by anionic exchange chromatography (DEAE-Sepharose column) and gel chromatography (Agarose-Heparin column) |
Herbaspirillum seropedicae |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.7.59 |
UTP + [protein-PII] |
GlnD of Herbaspirillum seropedicae is overexpressed with the two PII proteins GlnK and GlnB. Results show that GlnD uridylylates GlnB and GlnK trimers producing the forms PII(UMP)1, PII(UMP)2 and PII(UMP)3. GlnB is more efficiently uridylylated than GlnK |
Herbaspirillum seropedicae |
diphosphate + uridylyl-[protein-PII] |
- |
r |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.7.59 |
GlnD |
- |
Herbaspirillum seropedicae |
2.7.7.59 |
uridylyltransferase |
- |
Herbaspirillum seropedicae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.7.7.59 |
7.5 |
- |
assay at |
Herbaspirillum seropedicae |