The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity
Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-c...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Limphong, Pattraranee [verfasserIn] McKinney, Ross M. [verfasserIn] Adams, Nicole E. [verfasserIn] Makaroff, Christopher A. [verfasserIn] Bennett, Brian [verfasserIn] Crowder, Michael W. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2009 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Journal of biological inorganic chemistry - Berlin : Springer, 1996, 15(2009), 2 vom: 16. Okt., Seite 249-258 |
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| Übergeordnetes Werk: |
volume:15 ; year:2009 ; number:2 ; day:16 ; month:10 ; pages:249-258 |
| Links: |
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| DOI / URN: |
10.1007/s00775-009-0593-6 |
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| Katalog-ID: |
SPR007740573 |
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| 245 | 1 | 4 | |a The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity |
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| 520 | |a Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. | ||
| 650 | 4 | |a Glyoxalase 2 |7 (dpeaa)DE-He213 | |
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| 650 | 4 | |a Iron |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Zinc |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Catalysis |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a McKinney, Ross M. |e verfasserin |4 aut | |
| 700 | 1 | |a Adams, Nicole E. |e verfasserin |4 aut | |
| 700 | 1 | |a Makaroff, Christopher A. |e verfasserin |4 aut | |
| 700 | 1 | |a Bennett, Brian |e verfasserin |4 aut | |
| 700 | 1 | |a Crowder, Michael W. |e verfasserin |4 aut | |
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| 952 | |d 15 |j 2009 |e 2 |b 16 |c 10 |h 249-258 | ||
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10.1007/s00775-009-0593-6 doi (DE-627)SPR007740573 (SPR)s00775-009-0593-6-e DE-627 ger DE-627 rakwb eng 570 ASE 540 ASE 35.79 bkl 35.49 bkl Limphong, Pattraranee verfasserin aut The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. Glyoxalase 2 (dpeaa)DE-He213 Metalloenzyme (dpeaa)DE-He213 Iron (dpeaa)DE-He213 Zinc (dpeaa)DE-He213 Catalysis (dpeaa)DE-He213 McKinney, Ross M. verfasserin aut Adams, Nicole E. verfasserin aut Makaroff, Christopher A. verfasserin aut Bennett, Brian verfasserin aut Crowder, Michael W. verfasserin aut Enthalten in Journal of biological inorganic chemistry Berlin : Springer, 1996 15(2009), 2 vom: 16. Okt., Seite 249-258 (DE-627)265506727 (DE-600)1464026-0 1432-1327 nnns volume:15 year:2009 number:2 day:16 month:10 pages:249-258 https://dx.doi.org/10.1007/s00775-009-0593-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.79 ASE 35.49 ASE AR 15 2009 2 16 10 249-258 |
| spelling |
10.1007/s00775-009-0593-6 doi (DE-627)SPR007740573 (SPR)s00775-009-0593-6-e DE-627 ger DE-627 rakwb eng 570 ASE 540 ASE 35.79 bkl 35.49 bkl Limphong, Pattraranee verfasserin aut The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. Glyoxalase 2 (dpeaa)DE-He213 Metalloenzyme (dpeaa)DE-He213 Iron (dpeaa)DE-He213 Zinc (dpeaa)DE-He213 Catalysis (dpeaa)DE-He213 McKinney, Ross M. verfasserin aut Adams, Nicole E. verfasserin aut Makaroff, Christopher A. verfasserin aut Bennett, Brian verfasserin aut Crowder, Michael W. verfasserin aut Enthalten in Journal of biological inorganic chemistry Berlin : Springer, 1996 15(2009), 2 vom: 16. Okt., Seite 249-258 (DE-627)265506727 (DE-600)1464026-0 1432-1327 nnns volume:15 year:2009 number:2 day:16 month:10 pages:249-258 https://dx.doi.org/10.1007/s00775-009-0593-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.79 ASE 35.49 ASE AR 15 2009 2 16 10 249-258 |
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10.1007/s00775-009-0593-6 doi (DE-627)SPR007740573 (SPR)s00775-009-0593-6-e DE-627 ger DE-627 rakwb eng 570 ASE 540 ASE 35.79 bkl 35.49 bkl Limphong, Pattraranee verfasserin aut The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. Glyoxalase 2 (dpeaa)DE-He213 Metalloenzyme (dpeaa)DE-He213 Iron (dpeaa)DE-He213 Zinc (dpeaa)DE-He213 Catalysis (dpeaa)DE-He213 McKinney, Ross M. verfasserin aut Adams, Nicole E. verfasserin aut Makaroff, Christopher A. verfasserin aut Bennett, Brian verfasserin aut Crowder, Michael W. verfasserin aut Enthalten in Journal of biological inorganic chemistry Berlin : Springer, 1996 15(2009), 2 vom: 16. Okt., Seite 249-258 (DE-627)265506727 (DE-600)1464026-0 1432-1327 nnns volume:15 year:2009 number:2 day:16 month:10 pages:249-258 https://dx.doi.org/10.1007/s00775-009-0593-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.79 ASE 35.49 ASE AR 15 2009 2 16 10 249-258 |
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10.1007/s00775-009-0593-6 doi (DE-627)SPR007740573 (SPR)s00775-009-0593-6-e DE-627 ger DE-627 rakwb eng 570 ASE 540 ASE 35.79 bkl 35.49 bkl Limphong, Pattraranee verfasserin aut The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. Glyoxalase 2 (dpeaa)DE-He213 Metalloenzyme (dpeaa)DE-He213 Iron (dpeaa)DE-He213 Zinc (dpeaa)DE-He213 Catalysis (dpeaa)DE-He213 McKinney, Ross M. verfasserin aut Adams, Nicole E. verfasserin aut Makaroff, Christopher A. verfasserin aut Bennett, Brian verfasserin aut Crowder, Michael W. verfasserin aut Enthalten in Journal of biological inorganic chemistry Berlin : Springer, 1996 15(2009), 2 vom: 16. Okt., Seite 249-258 (DE-627)265506727 (DE-600)1464026-0 1432-1327 nnns volume:15 year:2009 number:2 day:16 month:10 pages:249-258 https://dx.doi.org/10.1007/s00775-009-0593-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.79 ASE 35.49 ASE AR 15 2009 2 16 10 249-258 |
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10.1007/s00775-009-0593-6 doi (DE-627)SPR007740573 (SPR)s00775-009-0593-6-e DE-627 ger DE-627 rakwb eng 570 ASE 540 ASE 35.79 bkl 35.49 bkl Limphong, Pattraranee verfasserin aut The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. Glyoxalase 2 (dpeaa)DE-He213 Metalloenzyme (dpeaa)DE-He213 Iron (dpeaa)DE-He213 Zinc (dpeaa)DE-He213 Catalysis (dpeaa)DE-He213 McKinney, Ross M. verfasserin aut Adams, Nicole E. verfasserin aut Makaroff, Christopher A. verfasserin aut Bennett, Brian verfasserin aut Crowder, Michael W. verfasserin aut Enthalten in Journal of biological inorganic chemistry Berlin : Springer, 1996 15(2009), 2 vom: 16. Okt., Seite 249-258 (DE-627)265506727 (DE-600)1464026-0 1432-1327 nnns volume:15 year:2009 number:2 day:16 month:10 pages:249-258 https://dx.doi.org/10.1007/s00775-009-0593-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.79 ASE 35.49 ASE AR 15 2009 2 16 10 249-258 |
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English |
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Enthalten in Journal of biological inorganic chemistry 15(2009), 2 vom: 16. Okt., Seite 249-258 volume:15 year:2009 number:2 day:16 month:10 pages:249-258 |
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Enthalten in Journal of biological inorganic chemistry 15(2009), 2 vom: 16. Okt., Seite 249-258 volume:15 year:2009 number:2 day:16 month:10 pages:249-258 |
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Glyoxalase 2 Metalloenzyme Iron Zinc Catalysis |
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Journal of biological inorganic chemistry |
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Limphong, Pattraranee @@aut@@ McKinney, Ross M. @@aut@@ Adams, Nicole E. @@aut@@ Makaroff, Christopher A. @@aut@@ Bennett, Brian @@aut@@ Crowder, Michael W. @@aut@@ |
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Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. 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Limphong, Pattraranee |
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Limphong, Pattraranee ddc 570 ddc 540 bkl 35.79 bkl 35.49 misc Glyoxalase 2 misc Metalloenzyme misc Iron misc Zinc misc Catalysis The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity |
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570 ASE 540 ASE 35.79 bkl 35.49 bkl The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity Glyoxalase 2 (dpeaa)DE-He213 Metalloenzyme (dpeaa)DE-He213 Iron (dpeaa)DE-He213 Zinc (dpeaa)DE-He213 Catalysis (dpeaa)DE-He213 |
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Limphong, Pattraranee McKinney, Ross M. Adams, Nicole E. Makaroff, Christopher A. Bennett, Brian Crowder, Michael W. |
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Limphong, Pattraranee |
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metal ion requirements of arabidopsis thaliana glx2-2 for catalytic activity |
| title_auth |
The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity |
| abstract |
Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. |
| abstractGer |
Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. |
| abstract_unstemmed |
Abstract In an effort to better understand the structure, metal content, the nature of the metal centers, and enzyme activity of Arabidopsis thaliana Glx2-2, the enzyme was overexpressed, purified, and characterized using metal analyses, kinetics, and UV–vis, EPR, and 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless were separated during purification, and the differently colored fractions were found to contain different amounts of Fe and Zn(II). Spectroscopic analyses of the discrete fractions provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), and antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among the discrete Glx2-2-containing fractions. The individual steady-state kinetic constants varied among the fractionated species, depending on the number and type of metal ion present. Intriguingly, however, the catalytic efficiency constant, kcat/Km, was invariant among the fractions. The value of kcat/Km governs the catalytic rate at low, physiological substrate concentrations. We suggest that the independence of kcat/Km on the precise makeup of the active-site metal center is evolutionarily related to the lack of selectivity for either Fe versus Zn(II) or Fe(II) versus Fe(III), in one or more metal binding sites. |
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The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity |
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| score |
7.401737 |