Values CatLog read from this paper
Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
PMID 20690587doi:10.1021/bi101103sOpen 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 4 records (10 values) from this paper: WlbA from Pseudomonas aeruginosa, Thermus thermophilus.
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 |
|---|---|---|---|---|---|---|---|
| WlbA | Pseudomonas aeruginosa | UDP-N-acetyl-D-glucosaminuronic acid | 5.55 × 10³ | 0.25 | 2.2 × 10⁴ | pH 8.5, 25 °C | Open record: WlbA, UDP-N-acetyl-D-glucosaminuronic acid |
| WlbA | Pseudomonas aeruginosa | α-ketoglutarate | — | 1.35 | 4.1 × 10³ | pH 8.5, 25 °C | Open record: WlbA, α-ketoglutarate |
| WlbA | Thermus thermophilus | UDP-N-acetyl-D-glucosaminuronic acid | 240 | 0.43 | 560 | pH 8.5, 25 °C | Open record: WlbA, UDP-N-acetyl-D-glucosaminuronic acid |
| WlbA | Thermus thermophilus | α-ketoglutarate | — | 2.35 | 100 | pH 8.5, 25 °C | Open record: WlbA, α-ketoglutarate |