Values CatLog read from this paper
Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy
PMID 14529297doi:10.1021/bi0344578Open 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: medium-chain acyl-CoA dehydrogenase from Sus scrofa.
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 |
|---|---|---|---|---|---|---|---|
| medium-chain acyl-CoA dehydrogenase | Sus scrofa | n-octanoyl-CoAenzyme as purified (FAD); 1.3 nM enzyme | 18.8 | 0.0025 | 7.5 × 10³ | pH 7.6, 25 °C | Open record: medium-chain acyl-CoA dehydrogenase, n-octanoyl-CoA |
| medium-chain acyl-CoA dehydrogenase | Sus scrofa | n-octanoyl-CoAenzyme reconstituted with commercial FAD (control) | 20 | 0.0026 | 7.7 × 10³ | pH 7.6, 25 °C | Open record: medium-chain acyl-CoA dehydrogenase, n-octanoyl-CoA |
| medium-chain acyl-CoA dehydrogenase | Sus scrofa | n-octanoyl-CoAenzyme reconstituted with the cofactor analogue 2′-deoxy-FAD | 0.047 | 0.0022 | 21 | pH 7.6, 25 °C | Open record: medium-chain acyl-CoA dehydrogenase, n-octanoyl-CoA |