Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Lyase
Reexamination Certificate
2005-11-22
2005-11-22
Saidha, Tekchand (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Lyase
C435S252300, C435S320100, C536S023200, C530S350000
Reexamination Certificate
active
06967097
ABSTRACT:
The present provides aRhodotorulaphenylalanine lyase polypeptide, polynucleotides that encode the polypeptide, and methods of obtaining and using these products. In particular the polypeptide can be employed for the production of phenylalanine, phenylalanine analogs, and optically active unnatural amino acids having phenylalanine-like structures.
REFERENCES:
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Bowie et al., 1990. Science, vo. 247, pp. 1306 1310.
Accession No. AAP80513 (PAL) and Applicants SEQ ID NO: 21 (PAL), are 89.9% identical [EP279655-A, Aug. 24, 1988].
Accession No. AAN81116 (DNA encoding PAL) and Applicants SEQ ID NO: 20 (DNA encoding PAL), are 67.8% identical [EP279665-A Aug. 24, 1988].
Accession No. E01783 (DNA encoding PAL) and Applicants' SEQ ID NO: 20, are 67.8% identical [JP 1988317086-A, Sep. 29, 1997].
Seffernick et al. [J. Bacteriol. Apr. 2001, p. 2406-2410].
Clara M. Ambrus, et al., “Phenylalanine Depletion for the Management of Phenylketonuria: Use of Enzyme Reactors with Immobilized Enzymes,”Science, 201:837-839, (1978).
John G. Anson, et al., “Complete nucleotide sequence of theRhodosporidium toruloidesgene coding for phenylalanine ammonia-lyase,”Gene, 58:189-199 (1987).
Godwin B D'Cunha, et al., “Stabilization of phenylalanine ammonia lyase containingRhodotorula glutiniscells for the continuous synthesis of L-phenylalanine methyl ester/96/,”Enzyme and Microbial Technology, 19:421-472, 1996.
Don R. Durham, et al., “Dissimilation of Aromatic Compounds inRhodotorula graminis: Biochemical Characterization of Pleiotropically Negative Mutants,”Journal of Bacteriology, 160:771-777, (1984).
Christopher T. Evans, et al., “BioConversion of Trans-Cinnamic Acid to L-Phenylalanine in an Immobilized Whole Cell Reactor,”Biotechnology and Bioengineering, 30:1067-1072 (1987).
James D. B. Faulkner, et al., “High-level expression of the phenylalanine ammonia lyase-encoding gene fromRhodosporidium toruloidesinSaccharomyces cerevisiaeandEscherichia coliusing bifunctional expression system,”Gene, 143(1):13-20 (1994).
David Filpula, et al., “Nucleotide sequence of gene for phenylalanine ammonia-lyase forRhodotorula rubra,”Nucleic Acids Research, 16:11381 (1988).
Andreas Gloge, et al., “Phenylalanine Ammonia-Lyase: The Use of Its Broad Substrate Specificty for Mechanistic Investigations and Biocatalysis—Synthesis of L-Arylalanines,”Chem. Eur. J.6:18, 3386-3390 (2000).
Daniel S. Hodgins, “Yeast Phenylalanine Ammonia-lyase, ”The Journal of Biological Chemistry, 246 (9):2977-2983 (1971).
Katsuhiko Nakamichi, et al., “Induction and Stabilization of L-Phenylalanine Ammonia-Lyase Activity inRhodotorula glutinis,”Eur. J. Appl. Microbiol Biotechnol, 18:158-162 (1983).
Derwent Abstract 85-095789 (Abstract to JP 83-151415).
JAPIO Abstract 81-026197 (Abstract to JP 56-26197).
JAPIO Abstract 88-148992 (Abstract to JP 63-148992).
GenBank Accession Nos. x13094 and x13095.
GenBank Accession Nos. x51513.
Kootstra Anna B.
Yoshida Roberta K.
PCBU Services, Inc.
Saidha Tekchand
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