Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots
The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC...
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| Autor*in: |
Marczewski, Waldemar [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1989 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Physiologia plantarum - Oxford [u.a.] : Wiley-Blackwell, 1948, 76(1989), 4, Seite 0 |
| Übergeordnetes Werk: |
volume:76 ; year:1989 ; number:4 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1111/j.1399-3054.1989.tb05475.x |
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| 245 | 1 | 0 | |a Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots |
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| 520 | |a The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. | ||
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10.1111/j.1399-3054.1989.tb05475.x doi (DE-627)NLEJ240958675 DE-627 ger DE-627 rakwb Marczewski, Waldemar verfasserin aut Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Enzyme kinetic In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 76(1989), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:76 year:1989 number:4 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05475.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 76 1989 4 0 |
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10.1111/j.1399-3054.1989.tb05475.x doi (DE-627)NLEJ240958675 DE-627 ger DE-627 rakwb Marczewski, Waldemar verfasserin aut Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Enzyme kinetic In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 76(1989), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:76 year:1989 number:4 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05475.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 76 1989 4 0 |
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10.1111/j.1399-3054.1989.tb05475.x doi (DE-627)NLEJ240958675 DE-627 ger DE-627 rakwb Marczewski, Waldemar verfasserin aut Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Enzyme kinetic In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 76(1989), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:76 year:1989 number:4 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05475.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 76 1989 4 0 |
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10.1111/j.1399-3054.1989.tb05475.x doi (DE-627)NLEJ240958675 DE-627 ger DE-627 rakwb Marczewski, Waldemar verfasserin aut Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Enzyme kinetic In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 76(1989), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:76 year:1989 number:4 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05475.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 76 1989 4 0 |
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10.1111/j.1399-3054.1989.tb05475.x doi (DE-627)NLEJ240958675 DE-627 ger DE-627 rakwb Marczewski, Waldemar verfasserin aut Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Enzyme kinetic In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 76(1989), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:76 year:1989 number:4 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05475.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 76 1989 4 0 |
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Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots |
| abstract |
The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. |
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The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. |
| abstract_unstemmed |
The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation. |
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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">NLEJ240958675</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707123220.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1989 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1399-3054.1989.tb05475.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240958675</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="100" ind1="1" ind2=" "><subfield code="a">Marczewski, Waldemar</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Kinetic properties of phosphoenolpyruvate carboxylase from lupin nodules and roots</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1989</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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">The kinetic properties of two forms of phosphoenolpyruvate carboxylase (PEPC I and PEPC II, EC 4.1, 1.31) from lupin (Lupinus luteus L. cv. Ventus) nodules and one enzyme form (PEPC III) from roots were studied. The Michaelis constant (Km) values for PEP, Mg2+ and especially HCO3−were lower for PEPC I. Kinetic studies showed that aspartate is a competitive inhibitor at pH 7.2 and inhibitor constant (Ki) values are different for the three forms of PEPC. Malate is a competitive inhibitor for PEPC I and PEPC III and shows mixed-type inhibition for PEPC II. Malate inhibition is dependent upon the pH of the assay. Different effect of several metabolites was also observed. The temperature optimum was near 39°C for PEPC I and around 43°C for PEPC II and PEPC III. PEPC I appeared to be the most thermolabile. It is suggested that PEPC I from lupin nodules is closely associated with N2 fixation.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzyme kinetic</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Physiologia plantarum</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1948</subfield><subfield code="g">76(1989), 4, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927738</subfield><subfield code="w">(DE-600)2020837-6</subfield><subfield code="x">1399-3054</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:76</subfield><subfield code="g">year:1989</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1399-3054.1989.tb05475.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</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-DJB</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">76</subfield><subfield code="j">1989</subfield><subfield code="e">4</subfield><subfield code="h">0</subfield></datafield></record></collection>
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