cofactors
(noun)
A substance, especially a coenzyme or a metal, that must be present for an enzyme to function.
Examples of cofactors in the following topics:
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Cofactors and Energy Transitions
- Cofactors are either organic or inorganic.
- An inactive enzyme without the cofactor is called an apoenzyme, while the complete enzyme with cofactor is the holoenzyme.
- Some enzymes or enzyme complexes require several cofactors.
- Organic cofactors are often vitamins or are made from vitamins.
- Cofactors can be divided into two broad groups: organic cofactors, such as flavin or heme, and inorganic cofactors, such as the metal ions Mg2+, Cu+, Mn2+, or iron-sulfur clusters.
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Cofactors, Minors, and Further Determinants
- The cofactor of an entry $(i,j)$ of a matrix $A$ is the signed minor of that matrix.
- Specifically the cofactor of the $(i,j)$ entry of a matrix, also known as the $(i,j)$ cofactor of that matrix, is the signed minor of that entry.
- The cofactor of $a_{ij}$ entry of a matrix is defined as:
- Note: If $i+j$ is an even number, the cofactor coincides with its minor: $C_{ij}=M_{ij}$.
- Explain how to use minor and cofactor matrices to calculate determinants
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Phenylketonuria (PKU)
- A rarer form of hyperphenylalaninemia occurs when PAH is normal, but there is a defect in the biosynthesis or recycling of the cofactor tetrahydrobiopterin (BH4) by the patient.
- This cofactor is necessary for proper activity of the enzyme.
- Dihydrobiopterin reductase activity is to replenish quinonoid-dihydrobiopterin back into its tetrahydrobiopterin form, which is an important cofactor in many metabolic reactions in amino acid metabolism.
- Those with this deficiency may produce sufficient levels of PAH, but since tetrahydrobiopterin is a cofactor for PAH activity, deficient dihydrobiopterin reductase renders any PAH enzyme non-functional.
- Tetrahydrobiopterin is also a cofactor in the production of L-DOPA from tyrosine and 5-hydroxy-l-tryptophan from tryptophan, which must also be supplemented as treatment in addition to the supplements for classical PKU.
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Control of Metabolism Through Enzyme Regulation
- Many enzymes only work if bound to non-protein helper molecules called cofactors and coenzymes.
- Cofactors are inorganic ions such as iron (Fe2+) and magnesium (Mg2+).
- Pyruvate dehydrogenase is a complex of several enzymes that requires one cofactor and five different organic coenzymes to catalyze its chemical reaction.
- The availability of various cofactors and coenzymes regulates enzyme function.
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Role of Vitamin K
- Coagulation is a complex cascade that requires many different cofactors and molecules to occur.
- Vitamin K, calcium, and phospholipids are necessary cofactors for proper coagulation, and people deficient in these substances will be more susceptible to uncontrolled bleeding.
- Calcium and phospholipids (a platelet membrane constituent) are required cofactors for prothrombin activation enzyme complexes to function.
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Nanoarchaeum and Aciduliprofundum
- N. equitans genome consists of a single circular chromosome, and lacks almost all genes required for synthesis of amino acids, nucleotides, cofactors, and lipids, but encodes everything needed for repair and replication. 95% of its DNA encodes for proteins for stable RNA molecules.
- Nanoarchaeum cannot synthesize most nucleotides, amino acids, lipids, and cofactors.
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Biomolecules
- Metalloprotein is a generic term for a protein that contains a metal ion cofactor.
- In addition to donor groups that are provided by amino acid residues, a large number of organic cofactors function as ligands.
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Enzyme Catalysis
- Covalent catalysis: covalent bonding to side chains or cofactors can lower the energy of the transition state.
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Iron-Binding Proteins
- They are carrier proteins (those used to move ions and molecules across membranes) and more generally metalloproteins (those which contain a metal ion cofactor).
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Gene Inversion
- For this to occur, there is typically one or more cofactors (to name a few: DNA-binding proteins and the presence or absence of DNA binding sites) and a site specific recombinase.