Values CatLog read from this paper
Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase
PMID 30142271doi:10.1021/acs.biochem.8b00811Open in Browse
The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.
CatLog read 5 records (13 values) from this paper: glutamine kinase (Cj1418) from Campylobacter jejuni.
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| glutamine kinase (Cj1418) | Campylobacter jejuni | D-glutamine | 1.5 | 10.5 | 0.14 | pH 8, 25 °C | 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 | 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 | Open record: glutamine kinase (Cj1418), L-glutamine |
| glutamine kinase (Cj1418) | Campylobacter jejuni | β-L-aspartyl hydroxamate | — | — | 0.0012 | pH 8, 25 °C | 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 | Open record: glutamine kinase (Cj1418), γ-L-glutamyl hydrazide |