Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8.

ABSTRACT:

Background

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.

Methodology/principal findings

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 structu

SUBMITTER: Igari S 

PROVIDER: S-EPMC3156243 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature