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
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1994 |
|---|
| Umfang: |
6 |
|---|
| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
|---|---|
| Übergeordnetes Werk: |
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 |
| Links: |
|---|
| Katalog-ID: |
NLEJ202739767 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ202739767 | ||
| 003 | DE-627 | ||
| 005 | 20230506010603.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070528s1994 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ202739767 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| 264 | 1 | |c 1994 | |
| 300 | |a 6 | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 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). | ||
| 533 | |f Springer Online Journal Archives 1860-2002 | ||
| 700 | 1 | |a Tokuyama, Shinji |4 oth | |
| 700 | 1 | |a Miya, Hiroyuki |4 oth | |
| 700 | 1 | |a Hatano, Kazunori |4 oth | |
| 700 | 1 | |a Takahashi, Takeshi |4 oth | |
| 773 | 0 | 8 | |i in |t Applied microbiology and biotechnology |d 1975 |g 40(1994) vom: Juni, Seite 835-840 |w (DE-627)NLEJ188988920 |w (DE-600)1464336-4 |x 1432-0614 |7 nnns |
| 773 | 1 | 8 | |g volume:40 |g year:1994 |g month:06 |g pages:835-840 |g extent:6 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1007/BF00173984 |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-SOJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 40 |j 1994 |c 6 |h 835-840 |g 6 | ||
| matchkey_str |
article:14320614:1994----::uiiainnpoeteoaoeezmnclmnaircmsf |
|---|---|
| hierarchy_sort_str |
1994 |
| publishDate |
1994 |
| allfields |
(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 |
| language |
English |
| source |
in Applied microbiology and biotechnology 40(1994) vom: Juni, Seite 835-840 volume:40 year:1994 month:06 pages:835-840 extent:6 |
| sourceStr |
in Applied microbiology and biotechnology 40(1994) vom: Juni, Seite 835-840 volume:40 year:1994 month:06 pages:835-840 extent:6 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Applied microbiology and biotechnology |
| authorswithroles_txt_mv |
Tokuyama, Shinji @@oth@@ Miya, Hiroyuki @@oth@@ Hatano, Kazunori @@oth@@ Takahashi, Takeshi @@oth@@ |
| publishDateDaySort_date |
1994-06-01T00:00:00Z |
| hierarchy_top_id |
NLEJ188988920 |
| id |
NLEJ202739767 |
| language_de |
englisch |
| fullrecord |
<?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>
|
| series2 |
Springer Online Journal Archives 1860-2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ188988920 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1432-0614 |
| topic_title |
Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
s t st h m hm k h kh t t tt |
| hierarchy_parent_title |
Applied microbiology and biotechnology |
| hierarchy_parent_id |
NLEJ188988920 |
| hierarchy_top_title |
Applied microbiology and biotechnology |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ188988920 (DE-600)1464336-4 |
| title |
Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| spellingShingle |
Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| ctrlnum |
(DE-627)NLEJ202739767 |
| title_full |
Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| journal |
Applied microbiology and biotechnology |
| journalStr |
Applied microbiology and biotechnology |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1994 |
| contenttype_str_mv |
zzz |
| container_start_page |
835 |
| container_volume |
40 |
| physical |
6 |
| format_se |
Elektronische Aufsätze |
| title_sort |
purification and properties of a novel enzyme, n-acylamino acid racemase, from streptomyces atratus y-53 |
| title_auth |
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). |
| collection_details |
GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE |
| title_short |
Purification and properties of a novel enzyme, N-acylamino acid racemase, from Streptomyces atratus Y-53 |
| url |
http://dx.doi.org/10.1007/BF00173984 |
| remote_bool |
true |
| author2 |
Tokuyama, Shinji Miya, Hiroyuki Hatano, Kazunori Takahashi, Takeshi |
| author2Str |
Tokuyama, Shinji Miya, Hiroyuki Hatano, Kazunori Takahashi, Takeshi |
| ppnlink |
NLEJ188988920 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth |
| up_date |
2024-07-06T08:44:07.300Z |
| _version_ |
1803818575908044800 |
| fullrecord_marcxml |
<?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>
|
| score |
7.3999834 |