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Literature summary for 1.6.3.4 extracted from

  • Zhou, Q.; Gao, J.; Zhang, Y.W.
    Optimal pH shift of the NADH oxidase from Lactobacillus rhamnosus with a single mutation (2021), Biotechnol. Lett., 43, 1413-1420 .
    View publication on PubMed
Search for more literature for 1.6.3.4

Protein Variants

Protein Variants Comment Organism
D170R 18.8% loss of activity Lacticaseibacillus rhamnosus
D219R 37.6% loss of activity Lacticaseibacillus rhamnosus
D247R 60.4% loss of activity Lacticaseibacillus rhamnosus
D251R mutation improves the activity to 112%, 111%, and 244% of the wild-type at pH 6.5, pH 7.0, and pH 7.5, respectively. NADH has access to the substrate-binding site with a larger substrate loop due to the enhanced electrostatic repulsion between Arg251 and Arg243. In the D251R-NADH complex, the carboxyl of NADH additionally forms two hydrogen bonds with G154 due to the changed interaction of substrate and the residues in the catalytic sites, and the hydrogen bond with the oxygen of carbonyl in P295 is shortened from 2.9 to 2.0 A Lacticaseibacillus rhamnosus
D359R 91% loss of activity Lacticaseibacillus rhamnosus
E316R 91% loss of activity Lacticaseibacillus rhamnosus

Organism

Organism UniProt Comment Textmining
Lacticaseibacillus rhamnosus
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
100.6
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 mutant D251R, pH 7, 2%°C Lacticaseibacillus rhamnosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 NADH + 2 H+ + O2
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 Lacticaseibacillus rhamnosus 2 NAD+ + 2 H2O
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