Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2002-10-02
2004-01-27
Saidha, Tekchand (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S252300, C435S320100, C530S350000, C536S023200
Reexamination Certificate
active
06682922
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to isolated polypeptides having lysophospholipase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
2. Description of the Related Art
Phospholipases are enzymes that participate in the hydrolysis of phospholipids which consist of a glycerol backbone with two fatty acids in an outer (sn-1) and the middle (sn-2) positions and esterified with phosphoric acid in the third position. The phosphoric acid may, in turn, be esterified to an amino alcohol.
Several types of phospholipase activity can be distinguished which hydrolyze the fatty acyl moieties. Phospholipase A1 and A2 catalyze the deacylation of one fatty acyl group in the sn-1 and sn-2 positions, respectively, from a diacylglycerophospholipid to produce lysophospholipid. Lysophospholipase (also called phospholipase B by the Nomenclature Committee of the International Union of Biochemistry on the Nomenclature and Classification of Enzymes {Enzyme Nomenclature, Academic Press, New York, 1992}) catalyzes the hydrolysis of the remaining fatty acyl group in a lysophospholipid. A phospholipase B has been reported from
Penicillium notatum
(Saito et al., 1991,
Methods in Enzymology
197:446-456) which catalyzes the deacylation of both fatty acids from a diacylglycerophospholipid and intrinsicly possesses lysophospholipase activity.
Fungal enzymes with phospholipase activity have been reported from various sources, including
Cryptococcus neoformans
(Chen et al., Infection and Immunity 65: 405-411),
Fusobacterium necrophorum
(Fifis et al., 1996
, Veterinary Microbiology
49: 219-233),
Penicillium notatum
(also known as
Penicillium chrysogenum;
Kawasaki, 1975
, Journal of Biochemistry
77: 1233-1244; Masuda et al., 1991
, European Journal of Biochemistry
202: 783-787),
Penicillium cyclopium
(Mustranta et al., 1995
, Process Biochemistry
30: 393-401),
Saccharomyces cerevisia
(Ichimasa et al., 1985
, Agric. Biol. Chem.
49: 1083-1089; Paultauf et al., 1994
, Journal of Biological Chemistry
269: 19725-19730),
Torulaspora delbrueckii
(old name
Saccharomyces rosei,
Kuwabara, 1988
, Agric. Biol. Chem.
52: 2451-2458; Watanabe et al., 1994
, FEMS Microbiological Letters
124: 29-34),
Schizosaccharomyces pombe
(Oishi et al., 1996
, Biosci. Biotech. Biochem.
60: 1087-1092),
Neurospora crassa
(Chakravarti et al., 1981
, Archives of Biochemistry and Biophysics
206: 393-402),
Aspergillus niger
(Technical Bulletin, G-zyme™ G6999, Enzyme Bio-Systems Ltd.; Mustranta et al., 1995, supra),
Corticium centrifugum
(Uehara et al., 1979
, Agric. Biol. Chem.
43: 517-525),
Fusarium oxysporum
(WO 98/26057), and
Fusarium solani
(Tsung-Che et al., 1968
, Phytopathological Notes
58:1437-38).
Fungal phospholipase genes have been cloned from several sources including
Penicillum notatum
(Masuda et al., 1991, supra),
Torulaspora delbrueckii
(Watanabe et al., 1994
, FEMS Microbiology Letters
124: 29-34),
Saccharomyces cerevisiae
(Lee at al., 1994
, Journal of Biological Chemistry
269: 19725-19730), Aspergillus (JP 10155493),
Neurospora crassa
(EMBL 042791), and
Schizosaccharomyces pombe
(EMBL 013857).
It is an object of the present invention to provide improved polypeptides having lysophospholipase activity and nucleic acid encoding the polypeptides.
SUMMARY OF THE INVENTION
The present invention relates to isolated polypeptides having lysophospholipase activity selected from the group consisting of:
(a) a polypeptide having an amino acid sequence which has at least 65% identity with amino acids 38 to 654 of SEQ ID NO. 2 or amino acids 17 to 648 of SEQ ID NO. 16;
(b) a polypeptide encoded by a nucleic acid sequence which hybridizes under high stringency conditions with (i) nucleotides 214 to 2061 of SEQ ID NO. 1 or nucleotides 49 to 1944 of SEQ ID NO. 15; (ii) the genomic DNA sequence containing nucleotides 214 to 2061 of SEQ ID NO. 1 or nucleotides 49 to 1944 of SEQ ID NO. 15; (iii) a subsequence of (i) or (ii) of at least 100 nucleotides; or (iv) a complementary strand of (i), (ii), or (iii);
(c) an allelic variant of (a) or (b); and
(d) a fragment of (a), (b) or (c), wherein the fragment has lysophospholipase activity.
The present invention also relates to isolated nucleic acid sequences encoding the polypeptides and to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
REFERENCES:
patent: 10155493 (1998-06-01), None
patent: WO 98/26057 (1998-06-01), None
Saito et al., 1991, Methods in Enzymology 197: 446-456.
Chen et al., 1997, Infection & Immunity 65: 405-411.
Fifis et al., 1996, Veterinary Microbiology 49: 219-233.
Kawaski, 1975, Journal of Biochemistry 77: 1233-1244.
Masuda et al., 1991, European Journal of Biochemistry 202: 783-787.
Mustranta et al., 1995, Process Biochemistry 30: 393-401.
Ichimasa et al., 1985, Agric. Biol. Chem. 49: 1083-1089.
Lee et al., 1994, Journal of Biological Chemistry 269: 19725-19730.
Kuwabara, 1998, Agric. Biol. Chem. 52: 2451-2458.
Watanabe et al., 1994, FEMS Microbiological Letters 124: 29-34.
Oishi et al., 1996, Biosci. Biotech. Biochem. 60:1087-1092.
Chakravarti et al., 1981, Archives of Biochemistry & Biophysics 206: 393-402.
Uehara et al., 1979, Agric. Biol. Chem. 43: 517-525.
Berka Randy M.
Byun Tony
Itami Ryoko
Klotz Alan
Rey Michael W.
Novozymes Biotech Inc.
Saidha Tekchand
Starnes Robert L.
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