R -hydroxynitrillyases having improved substrate tolerance...

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing nitrogen-containing organic compound

Reexamination Certificate

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C435S232000

Reexamination Certificate

active

07572608

ABSTRACT:
The invention relates to R-hydroxynitrillyases from the family of Rosaceae that are characterized by an improved substrate tolerance and increased stability. In the active center of the R-hydroxynitrillyases either a) an alanine group is substituted by glycine, valine, leucine, isoleucine, or phenylalanine or b) a phenylalanine group is substituted by alanine, glycine valine, leucine or isoleucine, or c) a leucine group is substituted by alanine, glycine, valine, isoleucine or phenylalanine, or d) an isoleucine group is substituted by alanine, glycine, valine, leucine or phenylalanine. The invention also relates to the use of these lyases in the production of enantiomer-pure R- or S-cyanohydrines.

REFERENCES:
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Glieder et al.(Angew. Chem.. Intl. ed. 2003, 42, 4815-4818).
Glieder et al. (Ang chem. Intl ed. 42, 4815-4818, 2003), In IDS.
Whisstock, et al. Quarterly Rev. Biophy. 2003, 36, pp. 307-340.
Ingrid Dreveny et al, The active site of hydroxynitrile lyase fromPrunus amygdalus: Modeling studies provide new insights into the mechanism of cyanogenesis; Feb. 2002, pp. 292-300, XP-002281486.
Ingrid Dreveny et al, The hydroxynitrile lyase from Almond: A Lyase that looks like an oxidoreductase; Sep. 2001; pp. 803-815; XP-002281487.
Herfried Griengl et al, The synthesis of chiral cyanohydrins by oxynitrilases; Jun. 2000; pp. 252-256; XP-002249789.
Anton Glieder et al, Comprehensive Step-by-Step Engineering of an (R)-Hydroxynitrile Lyase for Large-Scale Asymmetric Synthesis; Oct. 13, 2003; pp. 4815-4818; XP-002281488.

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