Values CatLog read from this paper
Kinetic, thermodynamic, and structural insight into the mechanism of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis
PMID 20851704doi:10.1016/j.jmb.2010.09.002Open 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 4 records (6 values) from this paper: phosphopantetheine adenylyltransferase (MtPPAT) from Mycobacterium tuberculosis.
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 2 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 |
|---|---|---|---|---|---|---|---|
| phosphopantetheine adenylyltransferase (MtPPAT) | Mycobacterium tuberculosis | 3'-dephospho-coenzyme A | 4.808 | 0.0067 | 720 calc. | pH 8, 25 °C | Open record: phosphopantetheine adenylyltransferase (MtPPAT), 3'-dephospho-coenzyme A |
| phosphopantetheine adenylyltransferase (MtPPAT) | Mycobacterium tuberculosis | 4'-phosphopantetheine | 4.853 | — | — | pH 7, 25 °C | Open record: phosphopantetheine adenylyltransferase (MtPPAT), 4'-phosphopantetheine |
| phosphopantetheine adenylyltransferase (MtPPAT) | Mycobacterium tuberculosis | adenosine 5'-triphosphateATP varied at 150 μM PhP | 4.547 | — | — | pH 7, 25 °C | Open record: phosphopantetheine adenylyltransferase (MtPPAT), adenosine 5'-triphosphate |
| phosphopantetheine adenylyltransferase (MtPPAT) | Mycobacterium tuberculosis | adenosine 5'-triphosphateATP varied at 25 μM PhP | 2.17 | 0.043 | 50 calc. | pH 7, 25 °C | Open record: phosphopantetheine adenylyltransferase (MtPPAT), adenosine 5'-triphosphate |