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Thermostable farnesyl dophosphate synthase of Bacillus stearothermophilus: crystalization and site-directed mutagenesis

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Koyama T., Obata S., Osabe M., Saito K., Takeshita A., Nishino T., Ogura K.

Acta Biochimica Polonica

1994

tom 41

nr 3

The gene for thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus was cloned, sequenced, and overexpressed in Escherichia coli. The synthase was purified to homogeneity and crystallized. The enzyme carried only two cysteine residues in contrast to its counterparts from other sources, which have four to six cysteine residues. Either or both of the cysteine residues can be replaced with serine without causing a loss of the catalytic activity. The conserved arginine residue that occupies the third position from the C-terminus was also replaced with valine without significant loss of activity, but the valine mutant showed a weakened affinity for isopentenyl diphosphate.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Koyama T.

1 Nishino T.

1 Obata S.

1 Ogura K.

1 Osabe M.

1 Saito K.

1 Takeshita A.

1 1994

Wyniki wyszukiwania

Thermostable farnesyl dophosphate synthase of Bacillus stearothermophilus: crystalization and site-directed mutagenesis