Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2001-09-19
2003-12-23
Slobodyansky, Elizabeth (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S252300, C435S252330, C435S254110, C435S254200, C435S320100, C435S325000, C435S069100, C435S069700, C435S410000, C536S023200, C536S023400, C536S023700
Reexamination Certificate
active
06667169
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to isolated polypeptides having acid phosphatase 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
Acid phosphatases (EC 3.1.3.2) catalyze the hydrolysis of an orthophosphate monoester to an alcohol and orthophosphate. The substrate specificity includes phosphomonoesters, nucleoside monophosphates, nucleoside diphosphates, nucleoside triphosphates, hexose monophosphates, and many other compounds (see, for example, Saha et al., 1985
, Archives of Biochemistry and Biophysics
243: 150-160; Gonzales and Meizel, 1973
, Biochimica Biophysica Acta
320: 180-194; Horgen et al., 1974
, Canadian Journal of Biochemistry
52: 126-136).
Acid phosphatases play a physiological role in fertilization (Lin and Clinton, 1987, In Merlevede and DiSalvo, editors,
Adv. Prof. Phosphatases
4: 199-228), epidermal growth (Lin and Clinton, 1987, supra), energy metabolism (Filburn, 1973
, Archives in Biochemistry and Biophysics
159: 683-693), mobilization of phosphorus reserves during seed germination (Ferens and Morawiecka, 1985
, Phytochemistry
24: 2839-2842); and scavenging phosphorus for growing cells (Heredia et al., 1963
, Biochem. Biophys. Res. Commun.
10: 14-18; Günther and Kattner, 1968
, Z. Naturforsch
236: 77-80; Roomans and Borst-Pauwels, 1979,
Biochemical Journal
178: 521-527).
Acid phosphatases have been reported to be useful for the preparation of nucleoside 5′-phosphates from a nucleoside and a phosphate donor (EP 857788).
Acid phosphatases have been isolated from mammals, plants, bacteria, yeast and fungi. In particular, acid phosphatases have been reportedly produced by Fusarium strains including
Fusarium culmorum
(Etebarian et al., 1996
, Iranian Journal of Plant Pathology
32: 9-21);
Fusarium solani
(Sano and Ui, 1981
, Annals of the Phytopathological Society of Japan
47: 547-554
; Fusarium oxysporum
(Madhosingh, 1980
, Phytopathologische Zeitschrift
97: 56-67);
Fusarium moniliforme
(Yoshida, 1973
, Journal of Biochemistry
73: 23-29); and Fusarium sp. (Huss et al., 1996
, Applied and Environmental Microbiology
62: 3750-3756; Min and Kweon, 1994
, Korean Journal of Mycology
22: 386-393; Pomazi et al., 1993
, Acta Microbiologica Hungarica
40: 71-79).
Acid phosphatase genes have been isolated from
Pichia pastoris
(U.S. Pat. No. 5,268,273) and
Saccharomyces cerevisiae
(Rodgers et al., 1982
, Proceedings of the National Academy of Sciences USA
79: 2157-2161).
There is a need in the art for new acid phosphatases that can be produced in commercial quantities.
It is an object of the present invention to provide improved polypeptides having acid phosphatase activity and nucleic acid encoding the polypeptides.
SUMMARY OF THE INVENTION
The present invention relates to isolated polypeptides having acid phosphatase activity selected from the group consisting of:
(a) a polypeptide having an amino acid sequence which has at least 65% identity with amino acids 19 to 318 of SEQ ID NO. 2;
(b) a polypeptide encoded by a nucleic acid sequence which hybridizes under medium stringency conditions with (i) nucleotides 138 to 1252 of SEQ ID NO. 1, (ii) the cDNA sequence contained in nucleotides 138 to 1252 of SEQ ID NO. 1, (iii) a subsequence of (i) or (ii) of at least 100 nucleotides, or (iv) a complementary strand of (i), (ii), or (iii);
(c) a variant of the polypeptide having an amino acid sequence of SEQ ID NO. 2 comprising a substitution, deletion, and/or insertion of one or more amino acids;
(d) an allelic variant of (a) or (b); and
(e) a fragment of (a), (b), or (d) that has acid phosphatase 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: 5268273 (1993-12-01), Buckholz
patent: 857788 (1998-12-01), None
Saha et al.. 1985. Archives of Biochemistry & Biophysics 243: 150-160.
Gonzales & Meizel. 1973. Biochemica Biophysica Acta 320: 180-194.
Horgen et al.. 1974. Canadian Journal of Biochemistry 52: 126-136.
Lin & Clinton, 1987, In Merlevede & DiSalvo, editors, Adv. Prot. Phosphatases 4: 199-228.
Filburn. 1973. Archives In Biochemistrv & Biophvsics 159: 683-693.
Ferens & Morawiecka. 1985. Phytochemistry 24: 2839-2842.
Heredia et al., 1963, BioChem. Biophys. Res. Commun. 10: 14-18.
Gunther & Kattner, 1968, Z. Naturforsch 236: 77-80.
Roomans & Borst-Pauwels, 1979, Biochemical Journal 178: 521-527.
Etebarian et al., 1996, Iranian Journal of Plant Pathology 32: 9-21.
Sano & Ui, 1981, Annals of Phytopathological Society of Japan 47: 547-554.
Madhosingh, 1980, Phytopathological Zeitschrift 97: 56-67.
Yoshida, 1973, Journal of Biochem 73: 23-29.
Huss et al., 1993, Applied & Enviro. Microbio. 62: 3750-3756.
Pomazi et al.. 1993. Acta Microbiological Hungarica 40: 71-79.
Rodgers et al., 1982, Proceedings of the National Academy of Science USA 79: 2757-2161.
Berka Randy M.
Rey Michael W.
Yaver Debbie S.
Novozymes Biotech Inc.
Slobodyansky Elizabeth
Starnes Robert L.
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