Values CatLog read from this paper
One-site polarity switch enhances catalytic efficiency and stability of D-allulose 3-epimerase via flexibility-rigidity rebalancing
PMID 42218266doi:10.1038/s41598-026-54479-zOpen 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 2 records (6 values) from this paper: D-allulose 3-epimerase (ApDAEase) from Arthrobacter psychrolactophilus.
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 |
|---|---|---|---|---|---|---|---|
| D-allulose 3-epimerase (ApDAEase) | Arthrobacter psychrolactophilus | D-fructose | 20.87 | 321.3 | 0.065 | pH 8.5, 70 °C | Open record: D-allulose 3-epimerase (ApDAEase), D-fructose |
| D-allulose 3-epimerase (ApDAEase)variant E35H | Arthrobacter psychrolactophilus | D-fructose | 22.75 | 248.8 | 0.0915 | pH 8.5, 70 °C | Open record: D-allulose 3-epimerase (ApDAEase) variant E35H, D-fructose |