Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53
Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 an...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Tokuyama, Shinji [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1994 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 1994 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 40(1994), 6 vom: Feb., Seite 835-840 |
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| Übergeordnetes Werk: |
volume:40 ; year:1994 ; number:6 ; month:02 ; pages:835-840 |
| Links: |
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| DOI / URN: |
10.1007/BF00173984 |
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| Katalog-ID: |
OLC2050671199 |
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| 245 | 1 | 0 | |a Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
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| 520 | |a Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). | ||
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| 700 | 1 | |a Miya, Hiroyuki |4 aut | |
| 700 | 1 | |a Hatano, Kazunori |4 aut | |
| 700 | 1 | |a Takahashi, Takeshi |4 aut | |
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10.1007/BF00173984 doi (DE-627)OLC2050671199 (DE-He213)BF00173984-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Tokuyama, Shinji verfasserin aut Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). Enzyme Streptomyces Divalent Metal Broad Substrate Specificity Relative Molecular Mass Miya, Hiroyuki aut Hatano, Kazunori aut Takahashi, Takeshi aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 40(1994), 6 vom: Feb., Seite 835-840 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:40 year:1994 number:6 month:02 pages:835-840 https://doi.org/10.1007/BF00173984 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 40 1994 6 02 835-840 |
| spelling |
10.1007/BF00173984 doi (DE-627)OLC2050671199 (DE-He213)BF00173984-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Tokuyama, Shinji verfasserin aut Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). Enzyme Streptomyces Divalent Metal Broad Substrate Specificity Relative Molecular Mass Miya, Hiroyuki aut Hatano, Kazunori aut Takahashi, Takeshi aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 40(1994), 6 vom: Feb., Seite 835-840 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:40 year:1994 number:6 month:02 pages:835-840 https://doi.org/10.1007/BF00173984 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 40 1994 6 02 835-840 |
| allfields_unstemmed |
10.1007/BF00173984 doi (DE-627)OLC2050671199 (DE-He213)BF00173984-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Tokuyama, Shinji verfasserin aut Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). Enzyme Streptomyces Divalent Metal Broad Substrate Specificity Relative Molecular Mass Miya, Hiroyuki aut Hatano, Kazunori aut Takahashi, Takeshi aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 40(1994), 6 vom: Feb., Seite 835-840 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:40 year:1994 number:6 month:02 pages:835-840 https://doi.org/10.1007/BF00173984 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 40 1994 6 02 835-840 |
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10.1007/BF00173984 doi (DE-627)OLC2050671199 (DE-He213)BF00173984-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Tokuyama, Shinji verfasserin aut Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). Enzyme Streptomyces Divalent Metal Broad Substrate Specificity Relative Molecular Mass Miya, Hiroyuki aut Hatano, Kazunori aut Takahashi, Takeshi aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 40(1994), 6 vom: Feb., Seite 835-840 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:40 year:1994 number:6 month:02 pages:835-840 https://doi.org/10.1007/BF00173984 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 40 1994 6 02 835-840 |
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10.1007/BF00173984 doi (DE-627)OLC2050671199 (DE-He213)BF00173984-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Tokuyama, Shinji verfasserin aut Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1994 Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). Enzyme Streptomyces Divalent Metal Broad Substrate Specificity Relative Molecular Mass Miya, Hiroyuki aut Hatano, Kazunori aut Takahashi, Takeshi aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 40(1994), 6 vom: Feb., Seite 835-840 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:40 year:1994 number:6 month:02 pages:835-840 https://doi.org/10.1007/BF00173984 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_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_130 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2006 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2021 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4028 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4103 GBV_ILN_4219 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4307 GBV_ILN_4310 AR 40 1994 6 02 835-840 |
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English |
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Enthalten in Applied microbiology and biotechnology 40(1994), 6 vom: Feb., Seite 835-840 volume:40 year:1994 number:6 month:02 pages:835-840 |
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Enthalten in Applied microbiology and biotechnology 40(1994), 6 vom: Feb., Seite 835-840 volume:40 year:1994 number:6 month:02 pages:835-840 |
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Enzyme Streptomyces Divalent Metal Broad Substrate Specificity Relative Molecular Mass |
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Tokuyama, Shinji @@aut@@ Miya, Hiroyuki @@aut@@ Hatano, Kazunori @@aut@@ Takahashi, Takeshi @@aut@@ |
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Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
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purification and properties of a novel enzyme, n-acylamino acid racemase, from streptomyces atratus y-53 |
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Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| abstract |
Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). © Springer-Verlag 1994 |
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Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). © Springer-Verlag 1994 |
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Abstract A novel enzyme, N-acylamino acid racemase, was purified to homogeneity from Streptomyces atratus Y-53 and characterized. This enzyme catalyzes the interconversion of optically active N-acylamino acids. The relative molecular mass ($ M_{r} $) of the enzyme was estimated to be about 41 000 and 244 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, respectively, indicating that the enzyme is composed of six subunits with an equal $ M_{r} $. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant ($ K_{m} $) values for N-acetyl-l-methionine and N-acetyl-d-methionine were calculated to be 15.2 and 5.6 mm, respectively. Enzyme activity was markedly enhanced by divalent metal ions, such as $ Co^{2+} $, $ Mg^{2+} $ and $ Mn^{2+} $, and was inhibited by metal-chelating reagent, indicating that the enzyme is a metalloenzyme. We propose to name the enzyme N-acylamino acid racemase (acylamino acid racemase). © Springer-Verlag 1994 |
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