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1.5.1.40: 8-hydroxy-5-deazaflavin:NADPH oxidoreductase

This is an abbreviated version!
For detailed information about 8-hydroxy-5-deazaflavin:NADPH oxidoreductase, go to the full flat file.

Word Map on EC 1.5.1.40

Reaction

reduced coenzyme F420
+
NADP+
=
oxidized coenzyme F420
 +
NADPH
 +
H+

Synonyms

5-deazaflavin-NADP+ reductase, 8-hydroxy-5-deazaflavin-dependent NADP+ reductase, 8-OH-5-deazaflavin:NADPH oxidoreductase, 8-OH-5dFl:NADPH oxidoreductase, AF0892, F420-dependent NADP oxidoreductase, F420-dependent NADP reductase, F420-dependent NADP+ oxidoreductase, F420:NADPH oxidoreductase, F420H2:NADP oxidoreductase, F420H2:NADP+ oxidoreductase, Fno, Msm_0049, NADP+:F420 oxidoreductase, Tfu-FNO, Tfu_0970

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.40 8-hydroxy-5-deazaflavin:NADPH oxidoreductase

Engineering

Engineering on EC 1.5.1.40 - 8-hydroxy-5-deazaflavin:NADPH oxidoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I135A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
I135G
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
I135V
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
G29L
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
G29S
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
G29Y
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
P89H
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
P89L
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
P89Y
site-directed mutagenesis, the mutant shows altered kinetics and increased catalytic efficiency with nicotinamide cofactor biomimetics compared to wild-type enzyme
R51A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R51E/R55A
site-directed mutagenesis, the mutant shows similar catalytic efficiency compared to the wild-type enzyme
R51E/R55N
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R51E/R55S
site-directed mutagenesis, the mutant shows similar catalytic efficiency compared to the wild-type enzyme
R51V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R51V/R55V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55N
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55S
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
R55V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
S50E
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
S50E/R55A
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
S50E/R55V
site-directed mutagenesis, the mutant shows slightly increased catalytic efficiency compared to the wild-type enzyme
S50Q
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A/R51V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A/R51V/R55V
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
T28A/R55A
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type enzyme
additional information