Values CatLog read from this paper
Increased structural flexibility at the active site of a fluorophore-conjugated beta-lactamase distinctively impacts its binding toward diverse cephalosporin antibiotics
PMID 21705325doi:10.1074/jbc.m110.198895Open 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 3 records (9 values) from this paper: PenPC beta-lactamase from Bacillus cereus.
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 |
|---|---|---|---|---|---|---|---|
| PenPC beta-lactamase | Bacillus cereus | penicillin G | 2612 | 0.048 | 5.4 × 10⁴ | pH 7 | Open record: PenPC beta-lactamase, penicillin G |
| PenPC beta-lactamasevariant E166C | Bacillus cereus | penicillin G | 2.1 | 0.072 | 29 | pH 7 | Open record: PenPC beta-lactamase variant E166C, penicillin G |
| PenPC beta-lactamasevariant E166C (BADAN-labeled; PenPC-E166Cb) | Bacillus cereus | penicillin G | 0.32 | 0.0079 | 40 | pH 7 | Open record: PenPC beta-lactamase variant E166C (BADAN-labeled; PenPC-E166Cb), penicillin G |