Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2007-06-12
2007-06-12
Saidha, Tekchand (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S252300, C435S320100, C435S019000, C536S023200
Reexamination Certificate
active
10450156
ABSTRACT:
The invention relates to biotechnologically expressible, enzymically active recombinant porcine liver esterases, to a biotechnological method for the preparation thereof and to the use thereof in organic synthesis. The monomeric subunits of recombinant porcine liver esterase are truncated at their C-terminal end, compared with naturally occurring porcine liver esterase subunits. Moreover, it has proved to be an additional advantage to truncate the N-terminal end as well.
REFERENCES:
patent: 00 04160 (2000-01-01), None
M. Matsushima et al.: “The nucleotide and deduced amino acid sequences of porcine liver proline- beta- naphthylamidase. Evidence for the identity with carboxylesterase” FEBS Letters, vol. 293, No. 1-2, pp. 37-41, Nov. 18, 1991.
L. David et al.: “Purification and molecular cloning of porcine intestinal glycerol-ester hydrolase-evidence for its identity with carboxylesterase” European Journal of Biochemistry, vol. 257, No. 1, pp. 142-148, Oct. 1, 1998.
J. Heim et al.: “Functional expression of a mammalian acetylcholinesterase in pichia pastorls: comparison to acetylcholinsterase, expressed and reconstituted fromEscherichia coli” Biochimica et Biophysica Acta, vol. 1396, No. 3, pp. 306-319, Mar. 13, 1998.
L. Giver et al.: “Direct evolution of a thermostable esterase” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, No. 22, pp. 12809-12813, Oct. 27, 1998.
Clustalw Result Clustal W (1.81) Multiple sequence alignments (2003).
S. Medda et al.: “The carboxylesterase family exhibits C-terminal sequence diversity reflecting the presence or absence of endoplasmic-reticulum-retention sequences” Eur J Biochem, vol. 206, No. 3, pp. 801-806, Jun. 15, 1992 (Abstract only).
M. Robbi et al.: “The COOH terminus of several liver caboxylesterases targets these enazymes to the lumen of the endoplasmic reticulum” J. Biol Chem, vol. 266, No. 30, pp. 20498-20503, Oct. 25, 2001 (Abstract only).
Bornscheuer Uwe
Lange Stefan
Musidlowska Anna
Schmidt-Dannert Claudia
Degussa - AG
Oblon & Spivak, McClelland, Maier & Neustadt P.C.
Saidha Tekchand
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