Values CatLog read from this paper
A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidase
PMID 15709736doi:10.1021/bi047989cOpen 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 5 records (9 values) from this paper: 5'-nucleotidase from Escherichia coli.
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 |
|---|---|---|---|---|---|---|---|
| 5'-nucleotidase | Escherichia coli | adenosine 5'-monophosphateTable 1 | 750 | 0.074 | 1.0 × 10⁴ calc. | pH 7.5, 25 °C | Open record: 5'-nucleotidase, adenosine 5'-monophosphate |
| 5'-nucleotidase | Escherichia coli | adenosine 5'-monophosphatein the text | — | 0.052 | — | pH 7.5, 25 °C | Open record: 5'-nucleotidase, adenosine 5'-monophosphate |
| 5'-nucleotidase | Escherichia coli | para-nitrophenyl phosphate | 60 | 4.741 | 13 calc. | pH 7.5, 25 °C | Open record: 5'-nucleotidase, para-nitrophenyl phosphate |
| 5'-nucleotidasevariant P90C/L424C | Escherichia coli | adenosine 5'-monophosphate | 313 | 0.011 | 2.8 × 10⁴ calc. | pH 7.5, 25 °C | Open record: 5'-nucleotidase variant P90C/L424C, adenosine 5'-monophosphate |
| 5'-nucleotidasevariant P90C/L424C | Escherichia coli | para-nitrophenyl phosphate | 350 | 5.355 | 65 calc. | pH 7.5, 25 °C | Open record: 5'-nucleotidase variant P90C/L424C, para-nitrophenyl phosphate |