Values CatLog read from this paper
Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation
PMID 16953590doi:10.1021/bi0607554Open 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 10 records (18 values) from this paper: phenylalanine hydroxylase (Δ117PheH), tryptophan hydroxylase (TrpH102–416) from Rattus norvegicus, Oryctolagus cuniculus.
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. CatLog calculated the 4 kcat/Km values marked “calc.” from kcat and Km; no printed kcat/Km was read for those records.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| phenylalanine hydroxylase (Δ117PheH) | Rattus norvegicus | 6-methyltetrahydropterin | — | 0.083 | — | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH), 6-methyltetrahydropterin |
| phenylalanine hydroxylase (Δ117PheH) | Rattus norvegicus | L-phenylalaninetyrosine formation (A275); 5 mM DTT | 8.55 | 0.12 | 72 | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH), L-phenylalanine |
| phenylalanine hydroxylase (Δ117PheH) | Rattus norvegicus | L-phenylalanine6-MePH4 oxidation; 200 µM 6-MePH4 (Table 1 footnote b) | 7.85 | 0.127 | 61.8 calc. | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH), L-phenylalanine |
| phenylalanine hydroxylase (Δ117PheH) | Rattus norvegicus | L-tryptophan200 µM 6-MePH4; 1.5 µM enzyme; 7 mM DTT; 50 µg/mL catalase | 0.55 | 0.7 | 0.79 calc. | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH), L-tryptophan |
| phenylalanine hydroxylase (Δ117PheH) | Rattus norvegicus | L-tryptophan6-MePH4 oxidation with L-tryptophan; 60 µg/mL catalase | 0.78 | 1 | 0.78 calc. | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH), L-tryptophan |
| phenylalanine hydroxylase (Δ117PheH)variant V379D | Rattus norvegicus | 6-methyltetrahydropterin | — | 0.063 | — | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH) variant V379D, 6-methyltetrahydropterin |
| phenylalanine hydroxylase (Δ117PheH)variant V379D | Rattus norvegicus | L-phenylalaninetyrosine formation (A275); 5 mM DTT | 0.3 | 0.42 | 0.72 | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH) variant V379D, L-phenylalanine |
| phenylalanine hydroxylase (Δ117PheH)variant V379D | Rattus norvegicus | L-phenylalanine6-MePH4 oxidation; 200 µM 6-MePH4 (Table 1 footnote b) | 1.12 | 0.625 | 1.80 calc. | pH 7, 25 °C | Open record: phenylalanine hydroxylase (Δ117PheH) variant V379D, L-phenylalanine |
| tryptophan hydroxylase (TrpH102–416) | Oryctolagus cuniculus | L-phenylalaninetyrosine formation (A275); 0.2 mM 6-MePH4; 5 mM DTT | 2.12 | — | — | pH 7, 25 °C | Open record: tryptophan hydroxylase (TrpH102–416), L-phenylalanine |
| tryptophan hydroxylase (TrpH102–416) | Oryctolagus cuniculus | L-phenylalanine6-MePH4 oxidation; 100-200 µM 6-MePH4 | 2.18 | — | — | pH 7, 25 °C | Open record: tryptophan hydroxylase (TrpH102–416), L-phenylalanine |