1.5.1.42: FMN reductase (NADH)
This is an abbreviated version!
For detailed information about FMN reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.42
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1.5.1.42
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luciferase
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monooxygenase
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desulfurization
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bioluminescent
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rhodococcus
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biodesulfurization
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erythropolis
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photobacterium
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dibenzothiophene
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fossil
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instantly
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p-hydroxyphenylacetate
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cost-competitive
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baumannii
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sigma54-dependent
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petroleum
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fmnh2-dependent
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phosphoreum
- 1.5.1.42
- luciferase
- monooxygenase
-
desulfurization
-
bioluminescent
- rhodococcus
-
biodesulfurization
- erythropolis
-
photobacterium
- dibenzothiophene
-
fossil
-
instantly
- p-hydroxyphenylacetate
-
cost-competitive
- baumannii
-
sigma54-dependent
-
petroleum
-
fmnh2-dependent
- phosphoreum
Reaction
Synonyms
DszD, flavin reductase, Fred, HcbA3, hexachlorobenzene oxidative dehalogenase system reductase component, LuxG, LuxG oxidoreductase, NADH specific FMN reductase, NADH-dependent FMN reductase, NADH-FMN oxidoreductase, NADH-FMN reductase, NADH:flavin oxidoreductase, NADH:FMN oxidoreductase, NADH:FMN oxidoreductase (flavin reductase), NADH:FMN-oxidoreductase
ECTree
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pH Range
pH Range on EC 1.5.1.42 - FMN reductase (NADH)
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5 - 10
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bimodal, pH 5: 90% of maximal activity, pH 6.5: about 50% of maximal activity, pH 10: about 70% of maximal activity
5 - 8.6
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the pH curve is bimodal, with maximal activity exhibited at pH 8.6, a minimum at pH 6.0. and a second maximum at pH 5.0
7 - 8.6
at pH 7.0, 7.2, and 8.0, the enzyme activity levels in 100 mM phosphate buffer are approx. 50.2, 88.1, and 81.1%, respectively, relative to that at pH 7.5. HcbA3C-His shows the highest flavin reductase activity in 60 mM KPi buffer