Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine
Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino aci...
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| Autor*in: |
Muramatsu, Hisashi [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2012 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag Berlin Heidelberg 2012 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 97(2012), 12 vom: 03. Okt., Seite 5389-5400 |
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| Übergeordnetes Werk: |
volume:97 ; year:2012 ; number:12 ; day:03 ; month:10 ; pages:5389-5400 |
| Links: |
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| DOI / URN: |
10.1007/s00253-012-4442-0 |
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| 520 | |a Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. | ||
| 650 | 4 | |a Ergothioneine | |
| 650 | 4 | |a Thiolurocanic acid | |
| 650 | 4 | |a Ergothionase | |
| 650 | 4 | |a Histidine ammonia-lyase | |
| 650 | 4 | |a Quantification of ergothioneine | |
| 700 | 1 | |a Matsuo, Hidenori |4 aut | |
| 700 | 1 | |a Okada, Naoki |4 aut | |
| 700 | 1 | |a Ueda, Momoko |4 aut | |
| 700 | 1 | |a Yamamoto, Hiroaki |4 aut | |
| 700 | 1 | |a Kato, Shin-ichiro |4 aut | |
| 700 | 1 | |a Nagata, Shinji |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Applied microbiology and biotechnology |d Springer-Verlag, 1984 |g 97(2012), 12 vom: 03. Okt., Seite 5389-5400 |w (DE-627)129942634 |w (DE-600)392453-1 |w (DE-576)015507750 |x 0175-7598 |7 nnns |
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10.1007/s00253-012-4442-0 doi (DE-627)OLC205075048X (DE-He213)s00253-012-4442-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Muramatsu, Hisashi verfasserin aut Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine 2012 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag Berlin Heidelberg 2012 Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. Ergothioneine Thiolurocanic acid Ergothionase Histidine ammonia-lyase Quantification of ergothioneine Matsuo, Hidenori aut Okada, Naoki aut Ueda, Momoko aut Yamamoto, Hiroaki aut Kato, Shin-ichiro aut Nagata, Shinji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 97(2012), 12 vom: 03. Okt., Seite 5389-5400 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 https://doi.org/10.1007/s00253-012-4442-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 AR 97 2012 12 03 10 5389-5400 |
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10.1007/s00253-012-4442-0 doi (DE-627)OLC205075048X (DE-He213)s00253-012-4442-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Muramatsu, Hisashi verfasserin aut Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine 2012 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag Berlin Heidelberg 2012 Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. Ergothioneine Thiolurocanic acid Ergothionase Histidine ammonia-lyase Quantification of ergothioneine Matsuo, Hidenori aut Okada, Naoki aut Ueda, Momoko aut Yamamoto, Hiroaki aut Kato, Shin-ichiro aut Nagata, Shinji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 97(2012), 12 vom: 03. Okt., Seite 5389-5400 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 https://doi.org/10.1007/s00253-012-4442-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 AR 97 2012 12 03 10 5389-5400 |
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10.1007/s00253-012-4442-0 doi (DE-627)OLC205075048X (DE-He213)s00253-012-4442-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Muramatsu, Hisashi verfasserin aut Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine 2012 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag Berlin Heidelberg 2012 Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. Ergothioneine Thiolurocanic acid Ergothionase Histidine ammonia-lyase Quantification of ergothioneine Matsuo, Hidenori aut Okada, Naoki aut Ueda, Momoko aut Yamamoto, Hiroaki aut Kato, Shin-ichiro aut Nagata, Shinji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 97(2012), 12 vom: 03. Okt., Seite 5389-5400 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 https://doi.org/10.1007/s00253-012-4442-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 AR 97 2012 12 03 10 5389-5400 |
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10.1007/s00253-012-4442-0 doi (DE-627)OLC205075048X (DE-He213)s00253-012-4442-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Muramatsu, Hisashi verfasserin aut Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine 2012 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag Berlin Heidelberg 2012 Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. Ergothioneine Thiolurocanic acid Ergothionase Histidine ammonia-lyase Quantification of ergothioneine Matsuo, Hidenori aut Okada, Naoki aut Ueda, Momoko aut Yamamoto, Hiroaki aut Kato, Shin-ichiro aut Nagata, Shinji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 97(2012), 12 vom: 03. Okt., Seite 5389-5400 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 https://doi.org/10.1007/s00253-012-4442-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 AR 97 2012 12 03 10 5389-5400 |
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10.1007/s00253-012-4442-0 doi (DE-627)OLC205075048X (DE-He213)s00253-012-4442-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Muramatsu, Hisashi verfasserin aut Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine 2012 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag Berlin Heidelberg 2012 Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. Ergothioneine Thiolurocanic acid Ergothionase Histidine ammonia-lyase Quantification of ergothioneine Matsuo, Hidenori aut Okada, Naoki aut Ueda, Momoko aut Yamamoto, Hiroaki aut Kato, Shin-ichiro aut Nagata, Shinji aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 97(2012), 12 vom: 03. Okt., Seite 5389-5400 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 https://doi.org/10.1007/s00253-012-4442-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 AR 97 2012 12 03 10 5389-5400 |
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Enthalten in Applied microbiology and biotechnology 97(2012), 12 vom: 03. Okt., Seite 5389-5400 volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 |
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Enthalten in Applied microbiology and biotechnology 97(2012), 12 vom: 03. Okt., Seite 5389-5400 volume:97 year:2012 number:12 day:03 month:10 pages:5389-5400 |
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Muramatsu, Hisashi @@aut@@ Matsuo, Hidenori @@aut@@ Okada, Naoki @@aut@@ Ueda, Momoko @@aut@@ Yamamoto, Hiroaki @@aut@@ Kato, Shin-ichiro @@aut@@ Nagata, Shinji @@aut@@ |
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HME13 and its application to enzymatic quantification of ergothioneine</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2012</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer-Verlag Berlin Heidelberg 2012</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. 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characterization of ergothionase from burkholderia sp. hme13 and its application to enzymatic quantification of ergothioneine |
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Characterization of ergothionase from Burkholderia sp. HME13 and its application to enzymatic quantification of ergothioneine |
| abstract |
Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. © Springer-Verlag Berlin Heidelberg 2012 |
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Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. © Springer-Verlag Berlin Heidelberg 2012 |
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Abstract We identified ergothionase, which catalyzes conversion of ergothioneine to thiolurocanic acid and trimethylamine, in a newly isolated ergothioneine-utilizing strain, Burkholderia sp. HME13. The enzyme was purified and its N-terminal amino acid sequence was determined. Based on the amino acid sequence, the gene encoding the enzyme was cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity and characterized. The enzyme consisted of four identical 55-kDa subunits. The enzyme showed maximum activity at pH 8.0 and 65 °C and was stable between pH 7.0 and pH 10.0 and up to 60 °C. The enzyme acted on ergothioneine (Km: 19 μM, Vmax: 270 μmol/min/mg), but not d-histidine, l-histidine, d-tyrosine, l-tyrosine, d-phenylalanine, or l-phenylalanine. The enzyme was activated by $ BaCl_{2} $ and strongly inhibited by $ CuSO_{4} $, $ ZnSO_{4} $, and $ HgCl_{2} $. The amino acid sequence of ergothionase showed 23 % similarity to histidine ammonia-lyase (HAL) from Pseudomonas putida and 17 % similarity to phenylalanine ammonia-lyase (PAL) from parsley. However, the tripeptide sequence, Ala-Ser-Gly, which is important for catalysis in both HAL and PAL, was not conserved in ergothionase. The application of ergothionase for the quantification of ergothioneine contained in practical food and blood samples was investigated by performing a recovery test. Satisfactory recovery data (98.7–104 %) were obtained when ergothioneine was added to extract of tamogitake and hemolysis blood. © Springer-Verlag Berlin Heidelberg 2012 |
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