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

• Autorzy: Koyama T. , Obata S. , Osabe M. , Saito K. , Takeshita A. , Nishino T. , Ogura K.
• Języki publikacji: EN

Abstrakty

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.

Słowa kluczowe

EN

Bacillus stearothermophilus; prenyltransferase; mutagenesis; farnesyl dophosphate synthase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1994
• Tom: 41
• Numer: 3
• Opis fizyczny: p.281-292,fig.

Twórcy

autor

Koyama T.

• Tokohu University, Sendai 980, Japan

autor

Obata S.

autor

Osabe M.

autor

Saito K.

autor

Takeshita A.

autor

Nishino T.

autor

Ogura K.

Bibliografia

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