ETFB Human
Description
Molecular Structure
ETFB Human is a 275-amino acid protein with a molecular mass of 30.0 kDa. The recombinant variant (PRO-220) includes an N-terminal His-tag and is expressed in E. coli . Key structural features include:
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Domains: Three distinct regions (I, II, III) with FAD bound between ETF-α and ETF-β subunits and AMP buried in domain III .
| Property | Details |
|---|---|
| Purity | >90% (SDS-PAGE) |
| Storage | 4°C (short-term), -20°C (long-term) |
| Buffer Composition | 20 mM Tris-HCl (pH 8.0), 40% glycerol |
Functional Role
ETF acts as an electron carrier in mitochondrial metabolism:
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Electron Transfer: Accepts electrons from 14+ flavoenzymes (e.g., acyl-CoA dehydrogenases, glutaryl-CoA dehydrogenase) and transfers them to ETF:ubiquinone oxidoreductase (ETFDH), feeding into the respiratory chain .
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Metabolic Pathways:
Key Interaction Partners:
| Protein | Function | Interaction Score |
|---|---|---|
| ETFDH | ETF-ubiquinone oxidoreductase; relays electrons to CoQ10 | 0.999 |
| ETFA | ETF-α subunit; stabilizes FAD binding | 0.999 |
| ACADM | Medium-chain acyl-CoA dehydrogenase; initiates fatty acid β-oxidation | 0.991 |
Clinical Significance
Mutations in ETFB cause multiple acyl-CoA dehydrogenase deficiency (MADD), an autosomal recessive disorder :
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Symptoms: Hypoglycemia, metabolic acidosis, organic aciduria (elevated glutaric, ethylmalonic acids).
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Diagnostic Markers:
Reported Pathogenic Mutations:
Research Applications
Recombinant ETFB Human (PRO-220) is widely used for:
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Enzyme Activity Assays: Measuring ETF-dependent dehydrogenase interactions .
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Structural Studies: Investigating conformational changes during electron transfer .
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Disease Modeling: Studying MADD pathogenesis and screening therapeutic compounds .
Pharmacological Status
As of 2025, no approved drugs target ETFB directly. Research focuses on:
Product Specs
KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE TTEDLVAKLK EIGRI.
Product Science Overview
ETFB is a heterodimeric protein composed of an alpha and beta subunit. The beta subunit, which is the focus here, contains an FAD (flavin adenine dinucleotide) cofactor and an AMP (adenosine monophosphate) molecule. These molecules are crucial for the protein’s function in electron transfer . The ETF complex accepts electrons from various mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, and transfers them to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase .
ETFB is involved in the metabolism of fatty acids and amino acids. It shuttles electrons between primary flavoprotein dehydrogenases and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. This process is vital for normal mitochondrial fatty acid oxidation and amino acid metabolism . Deficiencies in ETFB can lead to metabolic disorders such as Multiple Acyl-CoA Dehydrogenase Deficiency (MADD), also known as glutaric acidemia type II .
Recombinant ETFB is produced using recombinant DNA technology, which involves inserting the ETFB gene into a suitable expression system, such as E. coli, to produce the protein in large quantities. The recombinant protein is then purified using chromatographic techniques . This recombinant form is used in research to study the protein’s structure, function, and role in metabolic diseases.
Mutations in the ETFB gene can lead to severe metabolic disorders. For instance, MADD is characterized by the accumulation of organic acids and fatty acid metabolites in the body, leading to symptoms such as muscle weakness, hypoglycemia, and metabolic acidosis . Understanding the structure and function of ETFB is crucial for developing therapeutic strategies for these conditions.
Research on ETFB has provided insights into its role in mitochondrial function and its involvement in metabolic diseases. Studies have shown that ETFB binds an AMP molecule that likely has a structural role . Additionally, the three-dimensional structure of human ETFB has been resolved, providing a detailed understanding of its function at the molecular level .
