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 (Mr) of the enzyme was estimated to be about 41 000 and 244 0...
Ausführliche Beschreibung
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Englisch |
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1994 |
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6 |
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Springer Online Journal Archives 1860-2002 |
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in: Applied microbiology and biotechnology - 1975, 40(1994) vom: Juni, Seite 835-840 |
Übergeordnetes Werk: |
volume:40 ; year:1994 ; month:06 ; pages:835-840 ; extent:6 |
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NLEJ202739767 |
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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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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 Tokuyama, Shinji |4 oth | |
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700 | 1 | |a Hatano, Kazunori |4 oth | |
700 | 1 | |a Takahashi, Takeshi |4 oth | |
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(DE-627)NLEJ202739767 DE-627 ger DE-627 rakwb eng Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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 Online Journal Archives 1860-2002 Tokuyama, Shinji oth Miya, Hiroyuki oth Hatano, Kazunori oth Takahashi, Takeshi oth in Applied microbiology and biotechnology 1975 40(1994) vom: Juni, Seite 835-840 (DE-627)NLEJ188988920 (DE-600)1464336-4 1432-0614 nnns volume:40 year:1994 month:06 pages:835-840 extent:6 http://dx.doi.org/10.1007/BF00173984 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1994 6 835-840 6 |
spelling |
(DE-627)NLEJ202739767 DE-627 ger DE-627 rakwb eng Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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 Online Journal Archives 1860-2002 Tokuyama, Shinji oth Miya, Hiroyuki oth Hatano, Kazunori oth Takahashi, Takeshi oth in Applied microbiology and biotechnology 1975 40(1994) vom: Juni, Seite 835-840 (DE-627)NLEJ188988920 (DE-600)1464336-4 1432-0614 nnns volume:40 year:1994 month:06 pages:835-840 extent:6 http://dx.doi.org/10.1007/BF00173984 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1994 6 835-840 6 |
allfields_unstemmed |
(DE-627)NLEJ202739767 DE-627 ger DE-627 rakwb eng Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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 Online Journal Archives 1860-2002 Tokuyama, Shinji oth Miya, Hiroyuki oth Hatano, Kazunori oth Takahashi, Takeshi oth in Applied microbiology and biotechnology 1975 40(1994) vom: Juni, Seite 835-840 (DE-627)NLEJ188988920 (DE-600)1464336-4 1432-0614 nnns volume:40 year:1994 month:06 pages:835-840 extent:6 http://dx.doi.org/10.1007/BF00173984 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1994 6 835-840 6 |
allfieldsGer |
(DE-627)NLEJ202739767 DE-627 ger DE-627 rakwb eng Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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 Online Journal Archives 1860-2002 Tokuyama, Shinji oth Miya, Hiroyuki oth Hatano, Kazunori oth Takahashi, Takeshi oth in Applied microbiology and biotechnology 1975 40(1994) vom: Juni, Seite 835-840 (DE-627)NLEJ188988920 (DE-600)1464336-4 1432-0614 nnns volume:40 year:1994 month:06 pages:835-840 extent:6 http://dx.doi.org/10.1007/BF00173984 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1994 6 835-840 6 |
allfieldsSound |
(DE-627)NLEJ202739767 DE-627 ger DE-627 rakwb eng Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 1994 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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 Online Journal Archives 1860-2002 Tokuyama, Shinji oth Miya, Hiroyuki oth Hatano, Kazunori oth Takahashi, Takeshi oth in Applied microbiology and biotechnology 1975 40(1994) vom: Juni, Seite 835-840 (DE-627)NLEJ188988920 (DE-600)1464336-4 1432-0614 nnns volume:40 year:1994 month:06 pages:835-840 extent:6 http://dx.doi.org/10.1007/BF00173984 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 40 1994 6 835-840 6 |
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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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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). |
abstractGer |
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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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). |
abstract_unstemmed |
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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ202739767</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506010603.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s1994 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ202739767</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1994</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">6</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="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 (Mr) 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 Mr. The enzyme showed a broad substrate specificity toward N-acylamino acids, such as N-acetylmethionine, N-chloroacetylphenylalanine and N-chloroacetylvaline. The apparent Michaelis constant (Km) 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 Co2+, Mg2+ and Mn2+, 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).</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tokuyama, Shinji</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Miya, Hiroyuki</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hatano, Kazunori</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Takahashi, Takeshi</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Applied microbiology and biotechnology</subfield><subfield code="d">1975</subfield><subfield code="g">40(1994) vom: Juni, Seite 835-840</subfield><subfield code="w">(DE-627)NLEJ188988920</subfield><subfield code="w">(DE-600)1464336-4</subfield><subfield code="x">1432-0614</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:40</subfield><subfield code="g">year:1994</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:835-840</subfield><subfield code="g">extent:6</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF00173984</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">40</subfield><subfield code="j">1994</subfield><subfield code="c">6</subfield><subfield code="h">835-840</subfield><subfield code="g">6</subfield></datafield></record></collection>
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