Values CatLog read from this paper
The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization
PMID 31301348doi:10.1016/j.jsb.2019.07.006Open 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 (4 values) from this paper: malate dehydrogenase (LDH-like MalDH, I. isl MalDH) from Ignicoccus islandicus.
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 |
|---|---|---|---|---|---|---|---|
| malate dehydrogenase (LDH-like MalDH, I. isl MalDH) | Ignicoccus islandicus | oxaloacetate | 444 | 0.38 | 1.2 × 10³ | pH 7, 70 °C | Open record: malate dehydrogenase (LDH-like MalDH, I. isl MalDH), oxaloacetate |
| malate dehydrogenase (LDH-like MalDH, I. isl MalDH) | Ignicoccus islandicus | pyruvate | 8 | — | — | pH 6 | Open record: malate dehydrogenase (LDH-like MalDH, I. isl MalDH), pyruvate |