Values CatLog read from this paper
Investigation of metal binding and activation of Escherichia coli glyoxalase I: kinetic, thermodynamic and mutagenesis studies
PMID 14556652doi:10.1042/bj20030271Open in Browse
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CatLog read 4 records (12 values) from this paper: glyoxalase I (GlxI) 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.
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Open record |
|---|---|---|---|---|---|---|---|
| glyoxalase I (GlxI) | Escherichia coli | hemithioacetal formed between methylglyoxal and glutathione50 mM potassium phosphate (standard assay buffer) | 106 | 0.012 | 8.8 × 10³ | pH 6.6 | Open record: glyoxalase I (GlxI), hemithioacetal formed between methylglyoxal and glutathione |
| glyoxalase I (GlxI) | Escherichia coli | hemithioacetal formed between methylglyoxal and glutathioneMes buffer (instead of phosphate) | 60.2 | 0.01 | 6 × 10³ | pH 6.6 | Open record: glyoxalase I (GlxI), hemithioacetal formed between methylglyoxal and glutathione |
| glyoxalase I (GlxI) | Escherichia coli | hemithioacetal formed between methylglyoxal and glutathione50 mM potassium phosphate (standard assay buffer) | 55.7 | 0.01 | 5.6 × 10³ | pH 6.6 | Open record: glyoxalase I (GlxI), hemithioacetal formed between methylglyoxal and glutathione |
| glyoxalase I (GlxI) | Escherichia coli | hemithioacetal formed between methylglyoxal and glutathione50 mM potassium phosphate (standard assay buffer) | 21.4 | 0.0089 | 2.4 × 10³ | pH 6.6 | Open record: glyoxalase I (GlxI), hemithioacetal formed between methylglyoxal and glutathione |