Similarities between 3-hydroxybenzoate 4-monooxygenase and Oxidoreductase
3-hydroxybenzoate 4-monooxygenase and Oxidoreductase have 5 things in common (in Unionpedia): Cofactor (biochemistry), Enzyme, List of enzymes, Nicotinamide adenine dinucleotide phosphate, Oxygen.
Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's activity.
3-hydroxybenzoate 4-monooxygenase and Cofactor (biochemistry) · Cofactor (biochemistry) and Oxidoreductase ·
Enzyme
Enzymes are macromolecular biological catalysts.
3-hydroxybenzoate 4-monooxygenase and Enzyme · Enzyme and Oxidoreductase ·
List of enzymes
This page lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission numbering system.
3-hydroxybenzoate 4-monooxygenase and List of enzymes · List of enzymes and Oxidoreductase ·
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.
3-hydroxybenzoate 4-monooxygenase and Nicotinamide adenine dinucleotide phosphate · Nicotinamide adenine dinucleotide phosphate and Oxidoreductase ·
Oxygen
Oxygen is a chemical element with symbol O and atomic number 8.
3-hydroxybenzoate 4-monooxygenase and Oxygen · Oxidoreductase and Oxygen ·
The list above answers the following questions
- What 3-hydroxybenzoate 4-monooxygenase and Oxidoreductase have in common
- What are the similarities between 3-hydroxybenzoate 4-monooxygenase and Oxidoreductase
3-hydroxybenzoate 4-monooxygenase and Oxidoreductase Comparison
3-hydroxybenzoate 4-monooxygenase has 17 relations, while Oxidoreductase has 35. As they have in common 5, the Jaccard index is 9.62% = 5 / (17 + 35).
References
This article shows the relationship between 3-hydroxybenzoate 4-monooxygenase and Oxidoreductase. To access each article from which the information was extracted, please visit: