Recombinant Human MECR Protein: Properties & Research Applications

Recombinant Human MECR Protein is a key enzyme reagent supporting research into mitochondrial fatty acid synthesis, serving as a reliable tool for biochemical assays, pathway studies, and drug target investigations.

Protein Name

Mitochondrial trans-2-enoyl-CoA reductase (MECR)

Also Known As

NRBF-1; trans-2-enoyl-ACP reductase, mitochondrial

Species

Human (Homo sapiens)

Protein Type

Recombinant enzyme (oxidoreductase)

Biological Role

Catalyzes the final reduction step in mitochondrial fatty acid synthesis (mtFAS), reducing trans-2-enoyl thioesters using NADPH

Research Relevance

Implicated in neurodegeneration, metabolic regulation, and lipoic acid biosynthesis

SKU

rp366171

What Is MECR? Gene, Protein, and Biological Context

MECR (Mitochondrial Enoyl-CoA Reductase), also designated NRBF-1, encodes a mitochondrial matrix enzyme that is a central component of the mammalian mitochondrial fatty acid synthesis type II (mtFAS) pathway. Unlike the cytoplasmic fatty acid synthesis system, mtFAS operates in the mitochondrial matrix using acyl-carrier protein (ACP)-linked intermediates and produces octanoyl chains that serve as precursors for lipoic acid biosynthesis.

MECR catalyzes the NAD(P)H-dependent reduction of trans-2-enoyl thioesters, representing the final reductive step of each elongation cycle in mtFAS. This enzymatic activity is structurally and mechanistically conserved with the bacterial FabI enzyme family, underscoring the prokaryotic evolutionary origin of the mitochondrial fatty acid synthesis pathway.

Proper MECR function is essential for maintaining adequate levels of lipoic acid, an indispensable cofactor for key mitochondrial enzyme complexes including pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase. Disruption of MECR activity has therefore been linked to mitochondrial metabolic dysfunction and neurological disease.

Biochemical Properties of Recombinant Human MECR Protein

Recombinant Human MECR Protein is produced using recombinant expression systems to deliver a well-characterized, research-grade enzyme for in vitro applications. The recombinant form preserves the catalytic core of the native mitochondrial enzyme, enabling reliable reproduction of its biochemical activity in controlled experimental settings.

Key biochemical characteristics of MECR include its dependence on NADPH as the preferred electron donor for the reductive reaction, its specificity for trans-2-enoyl substrates linked via thioester bonds to ACP or CoA, and its localization signal that directs the native protein to the mitochondrial matrix. The recombinant protein is typically produced without the mitochondrial targeting sequence to facilitate heterologous expression and purification.

As a member of the short-chain dehydrogenase/reductase (SDR) superfamily, MECR shares conserved Rossmann-fold structural features that coordinate NAD(P)H binding. These structural characteristics make it a valuable model enzyme for structure-activity relationship studies and inhibitor screening campaigns targeting mitochondrial metabolism.

Research Applications of Recombinant Human MECR Protein

Recombinant Human MECR Protein supports a broad spectrum of research applications in cell biology, biochemistry, and translational medicine:

• Enzyme Activity Assays: The recombinant protein serves as a positive control or active enzyme source in NADPH-dependent enoyl reductase activity assays, enabling quantification of enzymatic kinetics and inhibitor potency.
• Drug Target Research: Given MECR's role in mtFAS and its structural similarity to FabI-family enzymes in bacteria, it represents a potential target for inhibitor development. Recombinant MECR is used in compound screening and mechanism-of-action studies.
• Mitochondrial Disease Research: MECR mutations have been associated with childhood-onset neurodegeneration with brain iron accumulation (NBIA-like phenotypes). The recombinant protein facilitates functional studies of disease-associated variants.
• Lipoic Acid Biosynthesis Studies: As mtFAS provides the octanoyl-ACP precursor for lipoic acid synthesis, MECR activity assays are integral to understanding lipoic acid metabolism and its links to mitochondrial enzyme complex function.
• Protein Interaction Studies: Recombinant MECR can be used in pull-down assays and co-immunoprecipitation experiments to map protein-protein interactions within the mtFAS complex.
• Western Blot and Immunoassay Standards: Purified recombinant protein serves as a molecular weight standard or antigen source for antibody validation.

Storage, Handling, and Quality Considerations

To maintain the activity and integrity of Recombinant Human MECR Protein, users should follow best practices for recombinant enzyme storage and handling:

• Storage Temperature: Recombinant proteins are generally stored at -80°C for long-term stability. Avoid repeated freeze-thaw cycles, which can cause protein aggregation and activity loss.
• Aliquoting: Upon first thaw, aliquot the protein into single-use volumes to minimize freeze-thaw degradation.
• Protein Concentration: Verify concentration by standard methods (e.g., BCA or Bradford assay) prior to use in quantitative experiments.
• Buffering Conditions: Ensure compatibility of the protein's formulation buffer with downstream assay conditions, particularly with respect to reducing agents and detergents that may affect enzyme activity.
• Quality Control: Research-grade recombinant proteins should be validated by SDS-PAGE for purity and by functional assay for activity prior to use in critical experiments.

Always consult the specific product datasheet (SKU: rp366171) for lot-specific specifications including purity, concentration, and recommended storage conditions.

Frequently asked questions

What is the biological function of the MECR protein?

MECR (Mitochondrial Enoyl-CoA Reductase) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in the mitochondrial fatty acid synthesis (mtFAS) type II pathway. This activity is essential for the biosynthesis of lipoic acid, a critical cofactor for several mitochondrial enzyme complexes.

What research applications is Recombinant Human MECR Protein suitable for?

Recombinant Human MECR Protein is suitable for enzyme activity assays, inhibitor screening, mitochondrial disease research, lipoic acid biosynthesis studies, protein-protein interaction studies, and use as a western blot standard or antigen for antibody validation.

How should Recombinant Human MECR Protein be stored to maintain activity?

The protein should be stored at -80°C for long-term stability. Repeated freeze-thaw cycles should be avoided; it is recommended to aliquot the protein into single-use volumes upon first thaw. Consult the product datasheet (SKU: rp366171) for lot-specific storage recommendations.

Is MECR related to any human diseases?

Yes, mutations in the MECR gene have been associated with childhood-onset neurodegeneration, including phenotypes resembling neurodegeneration with brain iron accumulation (NBIA). These disease associations make MECR an important subject of study in mitochondrial and neurological disease research.

What protein family does MECR belong to, and why is this significant?

MECR belongs to the short-chain dehydrogenase/reductase (SDR) superfamily and is structurally related to the bacterial FabI enzyme family. This structural conservation with bacterial enzymes highlights the evolutionary origin of mitochondrial fatty acid synthesis and positions MECR as a potential target for selective inhibitor design.

References

1. Autio KJ, et al. An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing. FASEB J. 2008.
2. Heimer G, et al. MECR mutations cause childhood-onset dystonia and optic atrophy, a mitochondrial fatty acid synthesis disorder. Am J Hum Genet. 2016.
3. Miinalainen IJ, et al. Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast Saccharomyces cerevisiae. J Biol Chem. 2003.

Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.