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6-Deoxyerythronolide B synthase and Oxidoreductase

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between 6-Deoxyerythronolide B synthase and Oxidoreductase

6-Deoxyerythronolide B synthase vs. Oxidoreductase

6-Deoxyerythronolide B Synthase or DEBS has been identified as a Type 1 polyketide synthase. In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor.

Similarities between 6-Deoxyerythronolide B synthase and Oxidoreductase

6-Deoxyerythronolide B synthase and Oxidoreductase have 3 things in common (in Unionpedia): Enzyme, Nicotinamide adenine dinucleotide phosphate, Redox.

Enzyme

Enzymes are macromolecular biological catalysts.

6-Deoxyerythronolide B synthase and Enzyme · Enzyme and Oxidoreductase · See more »

Nicotinamide adenine dinucleotide phosphate

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as lipid and nucleic acid synthesis, which require NADPH as a reducing agent.

6-Deoxyerythronolide B synthase and Nicotinamide adenine dinucleotide phosphate · Nicotinamide adenine dinucleotide phosphate and Oxidoreductase · See more »

Redox

Redox (short for reduction–oxidation reaction) (pronunciation: or) is a chemical reaction in which the oxidation states of atoms are changed.

6-Deoxyerythronolide B synthase and Redox · Oxidoreductase and Redox · See more »

The list above answers the following questions

6-Deoxyerythronolide B synthase and Oxidoreductase Comparison

6-Deoxyerythronolide B synthase has 63 relations, while Oxidoreductase has 35. As they have in common 3, the Jaccard index is 3.06% = 3 / (63 + 35).

References

This article shows the relationship between 6-Deoxyerythronolide B synthase and Oxidoreductase. To access each article from which the information was extracted, please visit:

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