Values CatLog read from this paper

Mechanistic and Molecular Dynamics Studies Reveal that Increased Loop 3 Mobility Alters Substrate Capture in an NADH:Quinone Oxidoreductase

PMID 41388968doi:10.1021/acs.biochem.5c00559Open 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 (10 values) from this paper: NADH:quinone oxidoreductase (NQO) from Pseudomonas aeruginosa.

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.

EC 1.6.5.9

Records read from this paper
EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsOpen record
NADH:quinone oxidoreductase (NQO)Pseudomonas aeruginosacoenzyme Q0110.035320pH 6, 25 °COpen record: NADH:quinone oxidoreductase (NQO), coenzyme Q0
NADH:quinone oxidoreductase (NQO)Pseudomonas aeruginosaNADH—4 × 10⁻⁴2.8 × 10⁴pH 6, 25 °COpen record: NADH:quinone oxidoreductase (NQO), NADH
NADH:quinone oxidoreductase (NQO)variant P78GPseudomonas aeruginosacoenzyme Q05.40.01560pH 6, 25 °COpen record: NADH:quinone oxidoreductase (NQO) variant P78G, coenzyme Q0
NADH:quinone oxidoreductase (NQO)variant P78GPseudomonas aeruginosaNADH—0.1343pH 6, 25 °COpen record: NADH:quinone oxidoreductase (NQO) variant P78G, NADH