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| Product | Description | |
|---|---|---|
| ferredoxin-NADP+ reductase | A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin. Group: Enzymes. Synonyms: ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+ oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase. Enzyme Commission Number: EC 1.18.1.2. CAS No. 9029-33-8. FNR. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1107; ferredoxin-NADP+ reductase; EC 1.18.1.2; 9029-33-8; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+ oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase. Cat No: EXWM-1107. |  |
| Native Spinacia oleracea (Spinach) Ferredoxin-NADP+ Reductase | Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria. Applications: Ferredoxin-nadp+ reductase was used in in vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. it was also used to regulate glyceraldehyde-3-phosphate dehydrogenase. Group: Enzymes. Synonyms: EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reducta. Enzyme Commission Number: EC 1.18.1.2. CAS No. 9029-33-8. FNR. Activity: > 15 units/mg solid, secondary activity: > 10 units/mg solid NADPH diaphorase. Storage: -20°C. Form: lyophilized powder. Source: Spinacia oleracea (Spinach). EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase; 9029-33-8; FNR. Cat No: NATE-0256. | |
| methionine synthase | Contains zinc and cobamide. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Reactivation by reductive methylation is catalysed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2, ferredoxin-NADP+ reductase). Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase, which acts only on the triglutamate. Group: Enzymes. Synonyms: 5-methyltetrahydrofolate-homocysteine S-methyltransferase; 5-methyltetrahydrofolate-homocysteine transmethy. Enzyme Commission Number: EC 2.1.1.13. CAS No. 9033-23-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1727; methionine synthase; EC 2.1.1.13; 9033-23-2; 5-methyltetrahydrofolate-homocysteine S-methyltransferase; 5-methyltetrahydrofolate-homocysteine transmethylase; N-methyltetrahydrofolate:L-homocysteine methyltransferase; N5-methyltetrahydrofolate methyltransferase; N5-methyltetrahydrofolate- | |
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