Article
Unique holoenzyme dimers of the tetrameric enzyme Escherichia coli methylenetetrahydrofolate reductase: characterization of structural features associated with modulation of the enzyme's function.
Biochemistry - 8 Apr 2003
Misra Sandeep K, Bhakuni Vinod
Abstract excerpt
Impaired functioning of methylenetetrahydrofolate reductase (MTHFR) can cause high levels of homocysteine in plasma or hyperhomocysteinemia, which is an independent risk factor for cardiovascular diseases and neural tube defects. We have studied in detail the effect of modulation of hydrophobic and electrostatic interactions of Escherichia coli MTHFR on its structure and function. Alterations in hydrophobic...
Topics
- Bacterial Proteins
- Chlorates
- Circular Dichroism
- Cross-Linking Reagents
- Dimerization
- Enzyme Stability
- Escherichia coli
- Flavin-Adenine Dinucleotide
- Glutaral
- Holoenzymes
- Hot Temperature
- Humans
- Methylenetetrahydrofolate Reductase (NADPH2)