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3-hydroxybenzyl-alcohol dehydrogenase is an enzyme that uses 3-hydroxybenzyl alcohol and NADP+ to produce 3-hydroxybenzaldehyde, NADPH and H+.
The enzyme 8-dimethylallylnaringenin 2'-hydroxylase uses sophoraflavanone B (8-prenylnaringenin), NADPH, H+ and O2 to produce leachianone G, NADP+ and H2O.
The enzyme dihydrokaempferol 4-reductase uses cis-3,4-leucopelargonidin and Dent corn
It is categorized as a species within the Family Poaceae, subfamily Panicoideae, and tribe Andropogoneae—a tribe of grasses that use the NADP–malic enzyme subtype of C4 photosynthesis in carbon fixation.
The enzyme Taxifolin 8-monooxygenase uses taxifolin, NADH, NADPH, H+, and O2 to produce 2,3-dihydrogossypetin, NAD+, NADP+, and H2O.
Flavanone 4-reductase is an enzyme that uses (2S)-flavan-4-ol and NADP+ to produce (2S)-flavanone, NADPH, and H+.
These studies took advantage of the fact that NAPDH, in its reduced form, is autofluorescent, and that metabolites such as glucose cause a predictable increase in NAPDH reduction.
Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.
The point on the curve where these two differing slopes meet is called the light saturation point and is where the light-dependent reactions are producing more ATP and NADPH than can be utilized by the light-independent reactions.
In contrast to MTHFD1 that has trifunctional methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase, and formyltetrahydrofolate synthetase enzymatic activities, MTHFD1L only has formyltetrahydrofolate synthetase activity.
Firstly, the NADPH used by pyocyanin depletes the available substrate for the reaction catalysed by the NADPH oxidase enzyme.
Usually, in the presence of NADPH dehydrogenase or NADH dehydrogenase as the enzyme, NADPH or NADH is the reductant that converts resazurin to resorufin.
Salutaridine synthase uses (R)-reticuline, NADPH, H+, and O2 to produce salutaridine, NADP+, and H2O.
In 1989, Israel Hanukoglu from the Weizmann Institute of Science discovered that the consensus sequence for NADP binding site in some enzymes that utilize NADP differs from the NAD binding motif.