Aug 23, 2011

Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8

PloS One
Sayaka IgariKazuhiro Yamada

Abstract

Methylenetetrahydrofolate reductase (MTHFR) is one of the enzymes involved in homocysteine metabolism. Despite considerable genetic and clinical attention, the reaction mechanism and regulation of this enzyme are not fully understood because of difficult production and poor stability. While recombinant enzymes from thermophilic organisms are often stable and easy to prepare, properties of thermostable MTHFRs have not yet been reported. MTHFR from Thermus thermophilus HB8, a homologue of Escherichia coli MetF, has been expressed in E. coli and purified. The purified MTHFR was chiefly obtained as a heterodimer of apo- and holo-subunits, that is, one flavin adenine dinucleotide (FAD) prosthetic group bound per dimer. The crystal structure of the holo-subunit was quite similar to the β(8)α(8) barrel of E. coli MTHFR, while that of the apo-subunit was a previously unobserved closed form. In addition, the intersubunit interface of the dimer in the crystals was different from any of the subunit interfaces of the tetramer of E. coli MTHFR. Free FAD could be incorporated into the apo-subunit of the purified Thermus enzyme after purification, forming a homodimer of holo-subunits. Comparison of the crystal structures of the heterodimer an...Continue Reading

Mentioned in this Paper

Formicum acidum, formic acid, Homeopathic preparation
Bacterial Proteins
Glycerin
Derivatives
expression vector
SDS-PAGE
Mthfr Activity
Methylenetetrahydrofolate Reductase (Nadph) Activity
Protein Structure, Quaternary
Thermus thermophilus extract

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