EC 2.7.3.13: glutamine kinase
TransferasesOpen in Browse
CatLog read 5 records for EC 2.7.3.13 from 1 paper, for 1 organism. Names in these papers: glutamine kinase (Cj1418).
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units.
CatLog also holds 4 records for EC 2.7.3.13 that are not yet re-read: from its earlier version, built from the enzyme databases and partly checked against the papers. All records for EC 2.7.3.13 in Browse.
Papers
| Paper | Organisms | Records |
|---|---|---|
| Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase | Campylobacter jejuni | 5 |
Records
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Paper | Open record |
|---|---|---|---|---|---|---|---|---|
| glutamine kinase (Cj1418) | Campylobacter jejuni | D-glutamine | 1.5 | 10.5 | 0.14 | pH 8, 25 °C | PMID 30142271 | Open record: glutamine kinase (Cj1418), D-glutamine |
| glutamine kinase (Cj1418) | Campylobacter jejuni | L-glutamic acid gamma-monohydroxamate | 2.1 | 1.5 | 1.4 | pH 8, 25 °C | PMID 30142271 | Open record: glutamine kinase (Cj1418), L-glutamic acid gamma-monohydroxamate |
| glutamine kinase (Cj1418) | Campylobacter jejuni | L-glutamine | 2.5 | 0.64 | 3.9 | pH 8, 25 °C | PMID 30142271 | Open record: glutamine kinase (Cj1418), L-glutamine |
| glutamine kinase (Cj1418) | Campylobacter jejuni | β-L-aspartyl hydroxamate | — | — | 0.0012 | pH 8, 25 °C | PMID 30142271 | Open record: glutamine kinase (Cj1418), β-L-aspartyl hydroxamate |
| glutamine kinase (Cj1418) | Campylobacter jejuni | γ-L-glutamyl hydrazide | 0.41 | 17.2 | 0.024 | pH 8, 25 °C | PMID 30142271 | Open record: glutamine kinase (Cj1418), γ-L-glutamyl hydrazide |