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

BRENDA support

Literature summary for 2.7.7.59 extracted from

  • Atkinson, M.R.; Ninfa, A.J.
    Characterization of the GlnK protein of Escherichia coli (1999), Mol. Microbiol., 32, 301-313.
    View publication on PubMed
Search for more literature for 2.7.7.59

Activating Compound

Activating Compound Comment Organism Structure
2-oxoglutarate at low concentration, required for PII uridylylation Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information GlnK protein-UMP is a very poor inhibitor of protein PII-UMP deuridylylation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII ?
-
 ?
UTP + [protein-GlnK] Escherichia coli enzyme regulates the regulatory GlnK protein diphosphate + uridylyl-[protein-GlnK]
-
 ir
UTP + [protein-PII] Escherichia coli the enzyme is involved in the cascade control of glutamine synthetase diphosphate + uridylyl-[protein-PII]
-
 r
UTP + [protein-PII] Escherichia coli enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation diphosphate + uridylyl-[protein-PII]
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII Escherichia coli ?
-
 ?
UTP + [protein-GlnK] regulatory protein Escherichia coli diphosphate + uridylyl-[protein-GlnK]
-
 ir
UTP + [protein-GlnK] GlnK protein mutant Y51N is no substrate Escherichia coli diphosphate + uridylyl-[protein-GlnK]
-
 ir
UTP + [protein-GlnK] very slow reverse reaction Escherichia coli diphosphate + uridylyl-[protein-GlnK]
-
 ir
UTP + [protein-GlnK] GlnK protein wild-type and mutant R47W Escherichia coli diphosphate + uridylyl-[protein-GlnK]
-
 ir
UTP + [protein-GlnK] enzyme regulates the regulatory GlnK protein Escherichia coli diphosphate + uridylyl-[protein-GlnK]
-
 ir
UTP + [protein-PII]
-
 Escherichia coli diphosphate + uridylyl-[protein-PII]
-
 r
UTP + [protein-PII] the enzyme is involved in the cascade control of glutamine synthetase Escherichia coli diphosphate + uridylyl-[protein-PII]
-
 r
UTP + [protein-PII] enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation Escherichia coli diphosphate + uridylyl-[protein-PII]
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli