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Literature summary for 2.7.7.59 extracted from
- Effects of T-loop modification on the PII-signalling protein structure of uridylylated Escherichia coli GlnB bound to ATP (2017), Environ. Microbiol. Rep., 9, 290-299 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene glnD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | recombinant production and purification of the uridylylating enzyme GlnD and its use for full uridylylation of large amounts of recombinantly produced pure EcGlnB | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diphosphate + uridylyl-[protein-PII] | Escherichia coli | - |
UTP + [protein-PII] | - |
r |  |
| UTP + [protein-PII] | Escherichia coli | - |
diphosphate + uridylyl-[protein-PII] | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P27249 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme GlnD from Escherichia coli strain BL21(DE3) | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diphosphate + uridylyl-[protein-PII GlnB] | substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnB | Escherichia coli | UTP + [protein-PII GlnK] | - |
r | |
| diphosphate + uridylyl-[protein-PII] | - |
Escherichia coli | UTP + [protein-PII] | - |
r | |
| additional information | the bifunctional enzyme GlnD catalyzes the uridylylation and, in the presence of glutamine, the deuridylylation of EcGlnB PII protein | Escherichia coli | ? | - |
- |
|
| UTP + [protein-PII GlnB] | the enzyme acts on residue Tyr51 of GlnK | Escherichia coli | diphosphate + uridylyl-[protein-PII GlnB] | - |
r | |
| UTP + [protein-PII] | - |
Escherichia coli | diphosphate + uridylyl-[protein-PII] | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlnD | - |
Escherichia coli |
| uridylylating enzyme | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | to adapt to environments with variable nitrogen sources and richness, the widely distributed homotrimeric PII signalling proteins bind their allosteric effectors ADP/ATP/2-oxoglutarate, and experience nitrogen-sensitive uridylylation of their flexible T-loops at Tyr51 by enzyme GlnD, regulating their interactions with effector proteins | Escherichia coli |
| additional information | crystal structure determination and analysis at 1.9 A resolution of the purified Escherichia coli GlnB (EcGlnB) PII protein in fully uridylylated form (EcGlnB-UMP3), structure-function analysis, overview. The T-loop is not visible. Unlike crystalline non-uridylylated EcGlnB, in which T-loops are fixed, uridylylation renders the T-loop highly mobile because of loss of contacts mediated by Tyr51, with concomitant abolition of T-loop anchoring via Arg38 on the ATP site. Analysis of mechanisms of PII selectivity for ATP and of PII-UMP3 signalling, proposing a model for the architecture of the complex of EcGlnBUMP3 with the uridylylation-sensitive PII target ATase (which adenylylates/deadenylylates glutamine synthetase [GS]) and with GS. Good X-ray diffracting crystals of trigonal shape and good size are obtained with fully uridylylated EcGlnB only when ATP, MgCl2 and 2-oxolutarate are present | Escherichia coli |
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