The Experts below are selected from a list of 15 Experts worldwide ranked by ideXlab platform
Daisuke Tsuru - One of the best experts on this subject based on the ideXlab platform.
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expression and secretion of <B>ScytalidopepsinB> B an acid protease from scytalidium lignicolum in yeast
Bioscience Biotechnology and Biochemistry, 2000Co-Authors: Ken Shimuta, Kohei Oda, Naoko Odaueda, Masahiro Washio, Hiroshi Oyama, Daisuke TsuruAbstract:An expression and secretion system for <B>ScytalidopepsinB> B, an acid protease from Scytalidium lignicolum, was constructed in yeast. Saccharomyces cerevisiae AH22 was transformed with an yeast-E. coli shuttle vector, pAM82, in which an yeast invertase signal segment and the cDNA encoding the pro- and mature enzyme regions were inserted. The transformant was found to secret a pepstatin-insensitive acid protease, when cultured aeroBically in a low phosphate (Pi) medium. Amino terminal amino acid sequencing analysis indicated that the recomBinant acid protease was accurately processed and secreted as a mature form.
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nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B <B>ScytalidopepsinB> B from scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1998Co-Authors: Naoko Oda, Kohei Oda, Hiroshi Oyama, Yoshikazu Gotoh, Sawao Murao, Daisuke TsuruAbstract:A chromosomal DNA of Scytalidium lignicolum was digested with Sau3AI. The digest was self-ligated and amplified By inverse PCR procedure using primers designed Based on the nucleotide sequences of up- and down-stream regions of an intron present in the <B>ScytalidopepsinB> B gene. Analysis of the nucleotide sequence of PCR product (700 Bp) showed that the enzyme is synthesized as a precursor protein consisting of the prepro- and mature enzyme regions. The deduced amino acid sequence was highly similar to those of aspergillopepsin A and recently reported endothiapepsins B and C, But quite different from those of pepstatin-insensitive Bacterial acid proteases and the pepstatin-sensitive aspartic protease family.
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nucleotide sequence of the gene encoding pepstatin insensitive acid protease B <B>ScytalidopepsinB> B of scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1996Co-Authors: Tsutomu Kakimori, Kohei Oda, Hiroshi Oyama, Naoko Oda, Yoshikazu Gotoh, Sawao Murao, Tadashi Yoshlmoto, Daisuke TsuruAbstract:A chromosomal DNA fragment of Scytalidium lignicolum that encodes the mature enzyme region of acid protease B (Scytalido-pepsin B), was cloned and its nucleotides sequenced. The fragment contained a 76-Bp intron at the middle of the mature enzyme-coding region. The mature enzyme was composed of 206 amino acid residues with a molecular weight of 21,550. There were some discrepancies Between the amino acid sequence deduced from these results and that previously estaBlished By protein sequencing.
Kohei Oda - One of the best experts on this subject based on the ideXlab platform.
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63 <B>ScytalidopepsinB> B
Handbook of Proteolytic Enzymes (Second Edition)#R##N#Aspartic and Metallo Peptidases, 2004Co-Authors: Kohei OdaAbstract:PuBlisher Summary This chapter focuses on the structural chemistry and the Biological aspects of <B>ScytalidopepsinB> B. This enzyme is one of the smallest carBoxyl proteinases active as a monomer. The pI is pH 3.2. The enzyme is a single polypeptide composed of 204 amino acid residues with a molecular weight of 21,969 Da. The amino acid sequence is quite different from those of pepstatin-sensitive carBoxyl proteinases such as pepsin and penicillopepsin. Unlike the other carBoxyl proteinases, one of the catalytic residues is glutamic acid. The active amino acid residue modified with l,2-epoxy-(p-nitrophenoxy)propane (EPNP) was found to Be Glu53. The other catalytic residue was found to Be Asp98. It is easy to distinguish this enzyme from the other pepstatininsensitive ones Because this enzyme is inhiBited By EPNP By using a new inhiBitor, l-diazo-3-phenyl-2-propanone. The amino acid sequence around Glu53 shows similarity to that around the active-site Asp215 residue of pig pepsin and other aspartic proteinases. While the amino acid sequence around Asp98 also shows similarity to that around the active Asp32, there is an insertion of a serine residue Between Thr and Gly.
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expression and secretion of <B>ScytalidopepsinB> B an acid protease from scytalidium lignicolum in yeast
Bioscience Biotechnology and Biochemistry, 2000Co-Authors: Ken Shimuta, Kohei Oda, Naoko Odaueda, Masahiro Washio, Hiroshi Oyama, Daisuke TsuruAbstract:An expression and secretion system for <B>ScytalidopepsinB> B, an acid protease from Scytalidium lignicolum, was constructed in yeast. Saccharomyces cerevisiae AH22 was transformed with an yeast-E. coli shuttle vector, pAM82, in which an yeast invertase signal segment and the cDNA encoding the pro- and mature enzyme regions were inserted. The transformant was found to secret a pepstatin-insensitive acid protease, when cultured aeroBically in a low phosphate (Pi) medium. Amino terminal amino acid sequencing analysis indicated that the recomBinant acid protease was accurately processed and secreted as a mature form.
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nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B <B>ScytalidopepsinB> B from scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1998Co-Authors: Naoko Oda, Kohei Oda, Hiroshi Oyama, Yoshikazu Gotoh, Sawao Murao, Daisuke TsuruAbstract:A chromosomal DNA of Scytalidium lignicolum was digested with Sau3AI. The digest was self-ligated and amplified By inverse PCR procedure using primers designed Based on the nucleotide sequences of up- and down-stream regions of an intron present in the <B>ScytalidopepsinB> B gene. Analysis of the nucleotide sequence of PCR product (700 Bp) showed that the enzyme is synthesized as a precursor protein consisting of the prepro- and mature enzyme regions. The deduced amino acid sequence was highly similar to those of aspergillopepsin A and recently reported endothiapepsins B and C, But quite different from those of pepstatin-insensitive Bacterial acid proteases and the pepstatin-sensitive aspartic protease family.
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nucleotide sequence of the gene encoding pepstatin insensitive acid protease B <B>ScytalidopepsinB> B of scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1996Co-Authors: Tsutomu Kakimori, Kohei Oda, Hiroshi Oyama, Naoko Oda, Yoshikazu Gotoh, Sawao Murao, Tadashi Yoshlmoto, Daisuke TsuruAbstract:A chromosomal DNA fragment of Scytalidium lignicolum that encodes the mature enzyme region of acid protease B (Scytalido-pepsin B), was cloned and its nucleotides sequenced. The fragment contained a 76-Bp intron at the middle of the mature enzyme-coding region. The mature enzyme was composed of 206 amino acid residues with a molecular weight of 21,550. There were some discrepancies Between the amino acid sequence deduced from these results and that previously estaBlished By protein sequencing.
Hiroshi Oyama - One of the best experts on this subject based on the ideXlab platform.
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expression and secretion of <B>ScytalidopepsinB> B an acid protease from scytalidium lignicolum in yeast
Bioscience Biotechnology and Biochemistry, 2000Co-Authors: Ken Shimuta, Kohei Oda, Naoko Odaueda, Masahiro Washio, Hiroshi Oyama, Daisuke TsuruAbstract:An expression and secretion system for <B>ScytalidopepsinB> B, an acid protease from Scytalidium lignicolum, was constructed in yeast. Saccharomyces cerevisiae AH22 was transformed with an yeast-E. coli shuttle vector, pAM82, in which an yeast invertase signal segment and the cDNA encoding the pro- and mature enzyme regions were inserted. The transformant was found to secret a pepstatin-insensitive acid protease, when cultured aeroBically in a low phosphate (Pi) medium. Amino terminal amino acid sequencing analysis indicated that the recomBinant acid protease was accurately processed and secreted as a mature form.
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nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B <B>ScytalidopepsinB> B from scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1998Co-Authors: Naoko Oda, Kohei Oda, Hiroshi Oyama, Yoshikazu Gotoh, Sawao Murao, Daisuke TsuruAbstract:A chromosomal DNA of Scytalidium lignicolum was digested with Sau3AI. The digest was self-ligated and amplified By inverse PCR procedure using primers designed Based on the nucleotide sequences of up- and down-stream regions of an intron present in the <B>ScytalidopepsinB> B gene. Analysis of the nucleotide sequence of PCR product (700 Bp) showed that the enzyme is synthesized as a precursor protein consisting of the prepro- and mature enzyme regions. The deduced amino acid sequence was highly similar to those of aspergillopepsin A and recently reported endothiapepsins B and C, But quite different from those of pepstatin-insensitive Bacterial acid proteases and the pepstatin-sensitive aspartic protease family.
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nucleotide sequence of the gene encoding pepstatin insensitive acid protease B <B>ScytalidopepsinB> B of scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1996Co-Authors: Tsutomu Kakimori, Kohei Oda, Hiroshi Oyama, Naoko Oda, Yoshikazu Gotoh, Sawao Murao, Tadashi Yoshlmoto, Daisuke TsuruAbstract:A chromosomal DNA fragment of Scytalidium lignicolum that encodes the mature enzyme region of acid protease B (Scytalido-pepsin B), was cloned and its nucleotides sequenced. The fragment contained a 76-Bp intron at the middle of the mature enzyme-coding region. The mature enzyme was composed of 206 amino acid residues with a molecular weight of 21,550. There were some discrepancies Between the amino acid sequence deduced from these results and that previously estaBlished By protein sequencing.
Naoko Oda - One of the best experts on this subject based on the ideXlab platform.
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nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B <B>ScytalidopepsinB> B from scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1998Co-Authors: Naoko Oda, Kohei Oda, Hiroshi Oyama, Yoshikazu Gotoh, Sawao Murao, Daisuke TsuruAbstract:A chromosomal DNA of Scytalidium lignicolum was digested with Sau3AI. The digest was self-ligated and amplified By inverse PCR procedure using primers designed Based on the nucleotide sequences of up- and down-stream regions of an intron present in the <B>ScytalidopepsinB> B gene. Analysis of the nucleotide sequence of PCR product (700 Bp) showed that the enzyme is synthesized as a precursor protein consisting of the prepro- and mature enzyme regions. The deduced amino acid sequence was highly similar to those of aspergillopepsin A and recently reported endothiapepsins B and C, But quite different from those of pepstatin-insensitive Bacterial acid proteases and the pepstatin-sensitive aspartic protease family.
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nucleotide sequence of the gene encoding pepstatin insensitive acid protease B <B>ScytalidopepsinB> B of scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1996Co-Authors: Tsutomu Kakimori, Kohei Oda, Hiroshi Oyama, Naoko Oda, Yoshikazu Gotoh, Sawao Murao, Tadashi Yoshlmoto, Daisuke TsuruAbstract:A chromosomal DNA fragment of Scytalidium lignicolum that encodes the mature enzyme region of acid protease B (Scytalido-pepsin B), was cloned and its nucleotides sequenced. The fragment contained a 76-Bp intron at the middle of the mature enzyme-coding region. The mature enzyme was composed of 206 amino acid residues with a molecular weight of 21,550. There were some discrepancies Between the amino acid sequence deduced from these results and that previously estaBlished By protein sequencing.
Yoshikazu Gotoh - One of the best experts on this subject based on the ideXlab platform.
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nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B <B>ScytalidopepsinB> B from scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1998Co-Authors: Naoko Oda, Kohei Oda, Hiroshi Oyama, Yoshikazu Gotoh, Sawao Murao, Daisuke TsuruAbstract:A chromosomal DNA of Scytalidium lignicolum was digested with Sau3AI. The digest was self-ligated and amplified By inverse PCR procedure using primers designed Based on the nucleotide sequences of up- and down-stream regions of an intron present in the <B>ScytalidopepsinB> B gene. Analysis of the nucleotide sequence of PCR product (700 Bp) showed that the enzyme is synthesized as a precursor protein consisting of the prepro- and mature enzyme regions. The deduced amino acid sequence was highly similar to those of aspergillopepsin A and recently reported endothiapepsins B and C, But quite different from those of pepstatin-insensitive Bacterial acid proteases and the pepstatin-sensitive aspartic protease family.
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nucleotide sequence of the gene encoding pepstatin insensitive acid protease B <B>ScytalidopepsinB> B of scytalidium lignicolum
Bioscience Biotechnology and Biochemistry, 1996Co-Authors: Tsutomu Kakimori, Kohei Oda, Hiroshi Oyama, Naoko Oda, Yoshikazu Gotoh, Sawao Murao, Tadashi Yoshlmoto, Daisuke TsuruAbstract:A chromosomal DNA fragment of Scytalidium lignicolum that encodes the mature enzyme region of acid protease B (Scytalido-pepsin B), was cloned and its nucleotides sequenced. The fragment contained a 76-Bp intron at the middle of the mature enzyme-coding region. The mature enzyme was composed of 206 amino acid residues with a molecular weight of 21,550. There were some discrepancies Between the amino acid sequence deduced from these results and that previously estaBlished By protein sequencing.