Any feedback?
Literature summary for 2.7.7.59 extracted from
- In vitro studies of the uridylylation of the three PII protein paralogs from Rhodospirillum rubrum: the transferase activity of R. rubrum GlnD is regulated by alpha-ketoglutarate and divalent cations but not by glutamine (2007), J. Bacteriol., 189, 3471-3478.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| (S)-N-dansyl-Tyr-Val-alpha-hydroxyglycine | plays a central role in uridylylation reaction, its required concentration for maximal uridylylation depends on the present cation | Rhodospirillum rubrum |  |
| ATP | required for uridylylation | Rhodospirillum rubrum | |
| L-glutamine | stimulates the deuridylylation reaction but in contrast to Escherichia coli glutamine has no effect on the uridylylation reaction | Rhodospirillum rubrum | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloned in Escherichia coli strain RB 9040 | Rhodospirillum rubrum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | in contrast to Escherichia coli the uridylylation reaction is not inhibited by glutamine | Rhodospirillum rubrum |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mn2+ | highest degree of uridylylation at 3 mM MnCl2 | Rhodospirillum rubrum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 105000 | - |
deduced from the gene sequence | Rhodospirillum rubrum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodospirillum rubrum | - |
S1 | - |
| Rhodospirillum rubrum S1 | - |
S1 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| GlnD is expressed as a GST-fusion protein | Rhodospirillum rubrum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UTP + [protein-PII] | bifunctional uridylyltransferase/uridylyl-removing enzyme, in Rhodospirillum rubrum three PII proteins have been identified GlnB, GlnK and GlnJ, respectively, in this study it is shown that all three PII proteins are uridylylated, although the efficacy is dependent on the cation present, Mn2+ or Mg2+, respectively | Rhodospirillum rubrum | diphosphate + uridylyl-[protein-PII] | - |
r | |
| UTP + [protein-PII] | bifunctional uridylyltransferase/uridylyl-removing enzyme, in Rhodospirillum rubrum three PII proteins have been identified GlnB, GlnK and GlnJ, respectively, in this study it is shown that all three PII proteins are uridylylated, although the efficacy is dependent on the cation present, Mn2+ or Mg2+, respectively | Rhodospirillum rubrum S1 | diphosphate + uridylyl-[protein-PII] | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlnD | - |
Rhodospirillum rubrum |
| GlnD | the bifunctional uridylyltransferase/uridylyl-removing enzyme is coded by the glnD gene in Rhodospirillum rubrum | Rhodospirillum rubrum |
| uridylyltransferase enzyme | - |
Rhodospirillum rubrum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Rhodospirillum rubrum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Rhodospirillum rubrum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
