Botryoccocus braunii triterpene synthase proteins and...

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing hydrocarbon

Reexamination Certificate

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C435S069100, C435S183000, C435S320100, C530S350000, C530S300000, C536S023200

Reexamination Certificate

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07985568

ABSTRACT:
This application relates to the functional identification and characterization of a nucleic acid molecule encoding a triterpene synthase, in particular botryococcene synthase. Also described are host cells comprising the nucleic acid molecules of this invention, proteins encoded by the nucleic acid molecules and methods for using the nucleic acid molecules, transformed hosts and encoded proteins to produce high levels of triterpene hydrocarbons.

REFERENCES:
Wells, Biochemistry, vol. 29, pp. 8509-8517, 1990.
Seffernick et al. (J. Bacteriology, vol. 183, pp. 2405-2410, 2001).
Blagg BSJ, Jarstfer MB, Rogers DH, Poulter CD (2002) Recombinant squalene synthase. A mechanism for the rearrangement of presqualene diphosphate to squalene. Journal of the American Chemical Society 124: 8846-8853.
Jarstfer MB, Zhang DL, Poulter CD (2002) Recombinant squalene synthase. Synthesis of non-head-to-tail isoprenoids in the absence of NADPH. Journal of the American Chemical Society 124: 8834-8845.
Poulter CD (1990) Biosynthesis of Non-Head-to-Tail Terpenes—Formation of 1′-1 and 1′-3 Linkages. Accounts of Chemical Research 23: 70-77.

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