Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2007-07-10
2007-07-10
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S252300, C435S071100
Reexamination Certificate
active
10181277
ABSTRACT:
The present invention relates to the expression and secretion inSaccharomyces cerevisiaeof readily purifiable soluble variants of the Kex1 endopeptidase ofKluyveromyces lactisand the purification and use thereof for the in vitro processing of recombinant proteins usable in industrial applications. The soluble Kex1 endoproteases described here are free from the transmembrane domain of the native enzyme; the deletion of the transmembrane domain is achieved by removing at least 57 amino acid residues from the C-terminal.
REFERENCES:
Tanguy-Rougeau TheKluyveromyces lactisKEX1 gene encodes a subtilisin-type serine proteinase. FEBS Lett. Jul. 18, 1988;234(2):464-70.
Wishart et al, A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J Biol Chem. Nov. 10, 1995;270(45):26782-26785.
Witkowski et al, Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine. Biochemistry. Sep. 7, 1999;38(36):11643-11650.
UniProt Database Accession No. P09231.
Latchinian-Sadek et al, Secretion, purification and characterization of a soluble form of the yeast KEX1-encoded protein from insect-cell cultures. Eur J Biochem. Jan. 15, 1994;219(1-2):647-52.
PIR—79 Database Accession No. KXBY from Mizuno et al Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases. Biochem Biophys Res Commun. Oct. 14, 1988;156(1):246-54. Alignment with SEQ ID No. 2.
Issued—Patents—AA Database from US5,935,815 van de Ven et al Mar. 8, 1999 SEQ ID No. 4. Alignment with SEQ ID No. 2.
Galye et al, Identification of regions in interleukin-1 alpha important for activity. J Biol Chem. Oct. 15, 1993;268(29):22105-11.
Whisstock et al, Prediction of protein function from protein sequence and structure. Q Rev Biophys. Aug. 2003;36(3):307-40. Review.
Davey et al., Isolation and characterization of krp, a dibasic endopeptidase required for cell viability in the fission yeastSchizosaccharomyces pombe. EMBO J. Dec. 15, 1994;13(24):5910-21.
Lee et al., Molecular characterization of KEX1, a kexin-like protease in mousePneumocystis carinii. Gene. Jan. 25, 2000;242(1-2):141-50.
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Orsini Gaetano
Taylor Geoffrey
Tonon Giancarlo
Tortora Paolo
Vanoni Marco
Darby & Darby
Keryos SpA
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