The cloning and sequencing of the genes encoding phytase ( phy ) and pH 2.5-optimum acid phosphatase ( aph ) from Aspergillus niger var. awamori
Identifieur interne : 004538 ( Main/Exploration ); précédent : 004537; suivant : 004539The cloning and sequencing of the genes encoding phytase ( phy ) and pH 2.5-optimum acid phosphatase ( aph ) from Aspergillus niger var. awamori
Auteurs : C. S. Piddington [États-Unis] ; C. S. Houston [États-Unis] ; M. Paloheimo ; M. Cantrell [États-Unis] ; A. Miettinen-Oinonen ; H. Nevalainen ; J. Rambosek [États-Unis]Source :
- Gene [ 0378-1119 ] ; 1993.
English descriptors
- Teeft :
- Acceptor sequences, Accession number, Acid phosphatase, Aspergillus, Aspergillus nidulans, Aspergillus niger, Awamori, Awamori strain, Boehringer mannheim, Cdna, Clone, Codon, Codon usage analysis, Degenerate, Degenerate oligo, Degenerate oligos, Encoding, Enzyme production, Extracellular, Extracellular phytase accounts, Further characterization, Gene, Gene encoding, Genes encoding phytase, Genomic, Genomic hybridizations, High frequency, Homology, Hybridization, Hybridizing plaques, Inorganic phosphorus, Inositol hexaphosphate, Intron, Intron donor, Niger, Nucleic acids, Nucleotide sequence, Oligo, Oligo probes, Peptide, Peptide 6tpho, Peptide sequence, Phosphatase, Phytase, Phytate, Plasmid, Preparative biochem, Primary structure, Restriction endonucleases, Sequencing, Signal peptide, Significant homology, Sphi, Sphi fragment, Structural gene, Turunen, Ullah.
Abstract
Abstract: The genes encoding phytase (EC 3.1.3.8) and pH 2.5-optimum acid phosphatase (EC 3.1.3.2) have been cloned and sequenced from Aspergillus niger var. awamori. The translated nucleotide sequences yielded polypeptides of 467 and 479 amino acids (aa) for phytase and acid phosphatase, respectively. The genes were isolated using oligodeoxyribonucleotide probes based on the aa sequences of the purified proteins. Recombinant A. niger var. awamori strains carrying additional copies of the gene sequences demonstrated elevated enzyme activities.
Url:
DOI: 10.1016/0378-1119(93)90224-Q
Affiliations:
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Rambosek</name><affiliation></affiliation><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Panlabs Incorporated, Bothell, WA 98011-8805</wicri:regionArea><wicri:noRegion>WA 98011-8805</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Gene</title><title level="j" type="abbrev">GENE</title><idno type="ISSN">0378-1119</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">133</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="55">55</biblScope><biblScope unit="page" to="62">62</biblScope></imprint><idno type="ISSN">0378-1119</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0378-1119</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acceptor sequences</term><term>Accession number</term><term>Acid phosphatase</term><term>Aspergillus</term><term>Aspergillus nidulans</term><term>Aspergillus niger</term><term>Awamori</term><term>Awamori strain</term><term>Boehringer mannheim</term><term>Cdna</term><term>Clone</term><term>Codon</term><term>Codon usage analysis</term><term>Degenerate</term><term>Degenerate oligo</term><term>Degenerate oligos</term><term>Encoding</term><term>Enzyme production</term><term>Extracellular</term><term>Extracellular phytase accounts</term><term>Further characterization</term><term>Gene</term><term>Gene encoding</term><term>Genes encoding phytase</term><term>Genomic</term><term>Genomic hybridizations</term><term>High frequency</term><term>Homology</term><term>Hybridization</term><term>Hybridizing plaques</term><term>Inorganic phosphorus</term><term>Inositol hexaphosphate</term><term>Intron</term><term>Intron donor</term><term>Niger</term><term>Nucleic acids</term><term>Nucleotide sequence</term><term>Oligo</term><term>Oligo probes</term><term>Peptide</term><term>Peptide 6tpho</term><term>Peptide sequence</term><term>Phosphatase</term><term>Phytase</term><term>Phytate</term><term>Plasmid</term><term>Preparative biochem</term><term>Primary structure</term><term>Restriction endonucleases</term><term>Sequencing</term><term>Signal peptide</term><term>Significant homology</term><term>Sphi</term><term>Sphi fragment</term><term>Structural gene</term><term>Turunen</term><term>Ullah</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The genes encoding phytase (EC 3.1.3.8) and pH 2.5-optimum acid phosphatase (EC 3.1.3.2) have been cloned and sequenced from Aspergillus niger var. awamori. The translated nucleotide sequences yielded polypeptides of 467 and 479 amino acids (aa) for phytase and acid phosphatase, respectively. The genes were isolated using oligodeoxyribonucleotide probes based on the aa sequences of the purified proteins. Recombinant A. niger var. awamori strains carrying additional copies of the gene sequences demonstrated elevated enzyme activities.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Miettinen Oinonen, A" sort="Miettinen Oinonen, A" uniqKey="Miettinen Oinonen A" first="A." last="Miettinen-Oinonen">A. Miettinen-Oinonen</name><name sortKey="Nevalainen, H" sort="Nevalainen, H" uniqKey="Nevalainen H" first="H." last="Nevalainen">H. Nevalainen</name><name sortKey="Paloheimo, M" sort="Paloheimo, M" uniqKey="Paloheimo M" first="M." last="Paloheimo">M. 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