The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
The functional signifcance of tyrosine 207 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase was explored by examining the kinetic properties of the Tyr207Leu mutant. The variant enzyme retained the structural characteristics of the wild-type protein as indicated by circular dichroism, i...
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BMC
2010-01-01
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Series: | Biological Research |
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Online Access: | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602010000200007 |
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author | Cherie Andrade Carolina Sepulveda Emilio Cardemil Ana M Jabalquinto |
author_facet | Cherie Andrade Carolina Sepulveda Emilio Cardemil Ana M Jabalquinto |
author_sort | Cherie Andrade |
collection | DOAJ |
description | The functional signifcance of tyrosine 207 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase was explored by examining the kinetic properties of the Tyr207Leu mutant. The variant enzyme retained the structural characteristics of the wild-type protein as indicated by circular dichroism, intrinsic fuorescence spectroscopy, and gel-exclusion chromatography. Kinetic analyses of the mutated variant showed a 15-fold increase in Km CO2, a 32fold decrease in Vmax, and a 6-fold decrease in Km for phosphoenolpyruvate. These results suggest that the hydroxyl group of Tyr 207 may polarize CO2 and oxaloacetate, thus facilitating the carboxylation/decarboxylation steps. |
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id | doaj.art-2fca9c3cdd3846d1bf4695225cdf9b8e |
institution | Directory Open Access Journal |
issn | 0716-9760 0717-6287 |
language | English |
last_indexed | 2024-12-11T10:05:47Z |
publishDate | 2010-01-01 |
publisher | BMC |
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series | Biological Research |
spelling | doaj.art-2fca9c3cdd3846d1bf4695225cdf9b8e2022-12-22T01:11:56ZengBMCBiological Research0716-97600717-62872010-01-01432191195The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinaseCherie AndradeCarolina SepulvedaEmilio CardemilAna M JabalquintoThe functional signifcance of tyrosine 207 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase was explored by examining the kinetic properties of the Tyr207Leu mutant. The variant enzyme retained the structural characteristics of the wild-type protein as indicated by circular dichroism, intrinsic fuorescence spectroscopy, and gel-exclusion chromatography. Kinetic analyses of the mutated variant showed a 15-fold increase in Km CO2, a 32fold decrease in Vmax, and a 6-fold decrease in Km for phosphoenolpyruvate. These results suggest that the hydroxyl group of Tyr 207 may polarize CO2 and oxaloacetate, thus facilitating the carboxylation/decarboxylation steps.http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602010000200007Phosphoenolpyruvate carboxykinaseSaccharomyces cerevisiaeCO2 interaction |
spellingShingle | Cherie Andrade Carolina Sepulveda Emilio Cardemil Ana M Jabalquinto The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase Biological Research Phosphoenolpyruvate carboxykinase Saccharomyces cerevisiae CO2 interaction |
title | The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase |
title_full | The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase |
title_fullStr | The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase |
title_full_unstemmed | The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase |
title_short | The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase |
title_sort | role of tyrosine 207 in the reaction catalyzed by saccharomyces cerevisiae phosphoenolpyruvate carboxykinase |
topic | Phosphoenolpyruvate carboxykinase Saccharomyces cerevisiae CO2 interaction |
url | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602010000200007 |
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