Values CatLog read from this paper
Crystal structures of human Delta4-3-ketosteroid 5beta-reductase (AKR1D1) reveal the presence of an alternative binding site responsible for substrate inhibition
PMID 19075558doi:10.1021/bi801276hOpen in Browse
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CatLog read 3 records (9 values) from this paper: human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1) from Homo sapiens.
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 |
|---|---|---|---|---|---|---|---|
| human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1) | Homo sapiens | androstenedione | 0.013 | 3.66 × 10⁻⁴ | 35.5 | pH 7.3, 37 °C | Open record: human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1), androstenedione |
| human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1)variant V309F | Homo sapiens | androstenedione | 0.0425 | 0.01629 | 2.6 | pH 7.3, 37 °C | Open record: human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1) variant V309F, androstenedione |
| human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1)variant Y132F | Homo sapiens | androstenedione | 0.0405 | 9.74 × 10⁻⁴ | 41.5 | pH 7.3, 37 °C | Open record: human delta4-3-ketosteroid 5beta-reductase (h5beta-red, AKR1D1) variant Y132F, androstenedione |