Values CatLog read from this paper
Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-beta-farnesene synthase
PMID 12820883doi:10.1021/bi034410mOpen in Browse
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CatLog read 2 records (6 values) from this paper: aristolochene synthase from Penicillium roqueforti.
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 |
|---|---|---|---|---|---|---|---|
| aristolochene synthasevariant Y92A | Penicillium roqueforti | farnesyl pyrophosphate | 0.00137 | 0.0834 | 0.0165 | pH 7.5 | Open record: aristolochene synthase variant Y92A, farnesyl pyrophosphate |
| aristolochene synthasevariant Y92C | Penicillium roqueforti | farnesyl pyrophosphate | 4.91 × 10⁻⁴ | 0.05027 | 0.0102 | pH 7.5 | Open record: aristolochene synthase variant Y92C, farnesyl pyrophosphate |