Lipase variants

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

Reexamination Certificate

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C435S136000, C435S198000, C435S252300, C435S320100, C536S023200

Reexamination Certificate

active

10493210

ABSTRACT:
The invention relates to a lipase variant which can be prepared by carrying out, on the amino acid sequence of a starting lipase selected from the lipase homologous family I.1 or I.2, at least one amino acid substitution in those positions which correspond to the positions 17, 29, 30, 52, 86, 117, 122, 160, 163, 167, 265, 266, 286, 289 in the prototype lipase sequence SEQ ID NO: 1.

REFERENCES:
patent: 6551806 (2003-04-01), Stürmer
patent: 6596520 (2003-07-01), Friedrich et al.
patent: 1 069 183 (2001-01-01), None
patent: WO92/05249 (1992-04-01), None
patent: WO95/35381 (1995-12-01), None
patent: WO 00/05354 (2000-02-01), None
M. Nardin, et al., “Crystal Structure ofPseudomonas aeruginosaLipase in the Open Conformation,”J. Biol. Chem., vol. 275, No. 40, Oct. 6, 2003, pp. 31219-31225.
K. Liebeton, et al., “Directed Evolution of an Enantioselective Lipase,”Chemistry and Biology, vol. 7, 2000, pp. 709-718.
L. G. J. Frenken, et al., “Cloning of thePseudomonas glumaeLipase Gene and Determination of the Active Site Residues,”Applied and Environm. Microbiology, vol. 58, No. 12, 1992, pp. 3787-3791.
J. L. Arpigny, et al., “Bacterial Lipolytic Enzymes: Classification and Properties,”Biochem. J., vol. 343, 1999, pp. 177-183.
Hwang, B-Y., et al., “Computer-aided molecular modeling of the enantioselectivity ofPseudomonas cepacialipase toward γ- δ-lactones”, Journal of Molecular Catalysis B: Enzymatic (2000), vol. 10, pp. 223-231.
Tuomi, W.V., et al., “Molecular Basis for Enantioselectivity of Lipase fromPseudomonoas cepaciatoward Primary Alcohols. Modeling, Kinetics, and Chemical Modification of Tyr29 to Increase or Decrease Enantioselectivity”, J. Org. Chem. (1999), vol. 64, pp. 2638-2647.
Gentner, C., et al., “Primary alcohols in a ring structure: quantifying enantioselectivity ofPseudomonas cepacialipase by an in silico assay”, Colloids and Surfaces B: Biointerfaces (2002), vol. 26, pp. 57-66.
Schulz, T., et al., “Stereoselectivity ofPseudomonas cepacialipase toward secondary alcohols: A quantitative model”, Protein Science (2000), vol. 9, pp. 1053-1062.
Kim, M.H., et al., “Substitution of Glycine 275 by Glutamate (G275E) in Lipase ofBacillus stearothermophilusAffects Its Catalytic Activity and Enantio- and Chain Length Specificity”, J. Microbiol. Biotechnol. (2000), vol. 10, No. 5, pp. 764-769.

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