Values CatLog read from this paper
Allosteric regulation of pyruvate kinase enables efficient and robust gluconeogenesis by preventing metabolic conflicts and carbon overflow
PMID 39873491doi:10.1128/msystems.01131-24Open 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 2 records (2 values) from this paper: pyruvate kinase from Bacillus subtilis.
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 |
|---|---|---|---|---|---|---|---|
| pyruvate kinase | Bacillus subtilis | adenosine 5'-diphosphate | — | 1.01 | — | pH 7.5 | Open record: pyruvate kinase, adenosine 5'-diphosphate |
| pyruvate kinasevariant ΔECTD | Bacillus subtilis | adenosine 5'-diphosphate | — | 1.83 | — | pH 7.5 | Open record: pyruvate kinase variant ΔECTD, adenosine 5'-diphosphate |