878 lines
52 KiB
JavaScript
878 lines
52 KiB
JavaScript
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"input": "FN Thomson Reuters Web of Knowledge\u000aVR 1.0\u000aPT J\u000aAU Zelle, Rintze M.\u000a Harrison, Jacob C.\u000a Pronk, Jack T.\u000a van Maris, Antonius J. A.\u000aTI Anaplerotic Role for Cytosolic Malic Enzyme in Engineered Saccharomyces\u000a cerevisiae Strains\u000aSO APPLIED AND ENVIRONMENTAL MICROBIOLOGY\u000aVL 77\u000aIS 3\u000aBP 732\u000aEP 738\u000aDI 10.1128/AEM.02132-10\u000aPD FEB 2011\u000aPY 2011\u000aAB Malic enzyme catalyzes the reversible oxidative decarboxylation of\u000a malate to pyruvate and CO(2). The Saccharomyces cerevisiae MAE1 gene\u000a encodes a mitochondrial malic enzyme whose proposed physiological roles\u000a are related to the oxidative, malate-decarboxylating reaction. Hitherto,\u000a the inability of pyruvate carboxylase-negative (Pyc(-)) S. cerevisiae\u000a strains to grow on glucose suggested that Mae1p cannot act as a\u000a pyruvate-carboxylating, anaplerotic enzyme. In this study, relocation of\u000a malic enzyme to the cytosol and creation of thermodynamically favorable\u000a conditions for pyruvate carboxylation by metabolic engineering, process\u000a design, and adaptive evolution, enabled malic enzyme to act as the sole\u000a anaplerotic enzyme in S. cerevisiae. The Escherichia coli NADH-dependent\u000a sfcA malic enzyme was expressed in a Pyc(-) S. cerevisiae background.\u000a When PDC2, a transcriptional regulator of pyruvate decarboxylase genes,\u000a was deleted to increase intracellular pyruvate levels and cells were\u000a grown under a CO(2) atmosphere to favor carboxylation, adaptive\u000a evolution yielded a strain that grew on glucose (specific growth rate,\u000a 0.06 +/- 0.01 h(-1)). Growth of the evolved strain was enabled by a\u000a single point mutation (Asp336Gly) that switched the cofactor preference\u000a of E. coli malic enzyme from NADH to NADPH. Consistently, cytosolic\u000a relocalization of the native Mae1p, which can use both NADH and NADPH,\u000a in a pyc1,2 Delta pdc2 Delta strain grown under a CO(2) atmosphere, also\u000a enabled slow-growth on glucose. Although growth rates of these strains\u000a are still low, the higher ATP efficiency of carboxylation via malic\u000a enzyme, compared to the pyruvate carboxylase pathway, may contribute to\u000a metabolic engineering of S. cerevisiae for anaerobic, high-yield\u000a C(4)-dicarboxylic acid production.\u000aTC 0\u000aZ9 0\u000aSN 0099-2240\u000aUT WOS:000286597100004\u000aER\u000a\u000aPT J\u000aAU Zelle, Rintze M.\u000a Trueheart, Josh\u000a Harrison, Jacob C.\u000a Pronk, Jack T.\u000a van Maris, Antonius J. A.\u000aTI Phosphoenolpyruvate Carboxykinase as the Sole Anaplerotic Enzyme in\u000a Saccharomyces cerevisiae\u000aSO APPLIED AND ENVIRONMENTAL MICROBIOLOGY\u000aVL 76\u000aIS 16\u000aBP 5383\u000aEP 5389\u000aDI 10.1128/AEM.01077-10\u000aPD AUG 2010\u000aPY 2010\u000aAB Pyruvate carboxylase is the sole anaplerotic enzyme in glucose-grown\u000a cultures of wild-type Saccharomyces cerevisiae. Pyruvate\u000a carboxylase-negative (Pyc(-)) S. cerevisiae strains cannot grow on\u000a glucose unless media are supplemented with C(4) compounds, such as\u000a aspartic acid. In several succinate-producing prokaryotes,\u000a phosphoenolpyruvate carboxykinase (PEPCK) fulfills this anaplerotic\u000a role. However, the S. cerevisiae PEPCK encoded by PCK1 is repressed by\u000a glucose and is considered to have a purely decarboxylating and\u000a gluconeogenic function. This study investigates whether and under which\u000a conditions PEPCK can replace the anaplerotic function of pyruvate\u000a carboxylase in S. cerevisiae. Pyc(-) S. cerevisiae strains\u000a constitutively overexpressing the PEPCK either from S. cerevisiae or\u000a from Actinobacillus succinogenes did not grow on glucose as the sole\u000a carbon source. However, evolutionary engineering yielded mutants able to\u000a grow on glucose as the sole carbon source at a maximum specific growth\u000a rate of ca. 0.14 h(-1), one-half that of the (pyruvate\u000a carboxylase-positive) reference strain grown under the same conditions.\u000a Growth was dependent on high carbon dioxide concentrations, indicating\u000a that the reaction catalyzed by PEPCK operates near thermodynamic\u000a equilibrium. Analysis and reverse engineering of two independently\u000a evolved strains showed that single point mutations in pyruvate kinase,\u000a which competes with PEPCK for phosphoenolpyruvate, were sufficient to\u000a enable the use of PEPCK as the sole anaplerotic enzyme. The PEPCK\u000a reaction produces one ATP per carboxylation event, whereas the original\u000a route through pyruvate kinase and pyruvate carboxylase is ATP neutral.\u000a This increased ATP yield may prove crucial for engineering of efficient\u000a and low-cost anaerobic production of C(4) dicarboxylic acids in S.\u000a cerevisiae.\u000aTC 1\u000aZ9 1\u000aSN 0099-2240\u000aUT WOS:000280633400006\u000aER\u000a\u000aPT J\u000aAU Zelle, Rintze M.\u000a De Hulster, Erik\u000a Kloezen, Wendy\u000a Pronk, Jack T.\u000a van Maris, Antonius J. A.\u000aTI Key Process Conditions for Production of C(4) Dicarboxylic Acids in\u000a Bioreactor Batch Cultures of an Engineered Saccharomyces cerevisiae\u000a Strain\u000aSO APPLIED AND ENVIRONMENTAL MICROBIOLOGY\u000aVL 76\u000aIS 3\u000aBP 744\u000aEP 750\u000aDI 10.1128/AEM.02396-09\u000aPD FEB 2010\u000aPY 2010\u000aAB A recent effort to improve malic acid production by Saccharomyces\u000a cerevisiae by means of metabolic engineering resulted in a strain that\u000a produced up to 59 g liter(-1) of malate at a yield of 0.42 mol (mol\u000a glucose)(-1) in calcium carbonate-buffered shake flask cultures. With\u000a shake flasks, process parameters that are important for scaling up this\u000a process cannot be controlled independently. In this study, growth and\u000a product formation by the engineered strain were studied in bioreactors\u000a in order to separately analyze the effects of pH, calcium, and carbon\u000a dioxide and oxygen availability. A near-neutral pH, which in shake\u000a flasks was achieved by adding CaCO(3), was required for efficient C(4)\u000a dicarboxylic acid production. Increased calcium concentrations, a side\u000a effect of CaCO(3) dissolution, had a small positive effect on malate\u000a formation. Carbon dioxide enrichment of the sparging gas (up to 15%\u000a [vol/vol]) improved production of both malate and succinate. At higher\u000a concentrations, succinate titers further increased, reaching 0.29 mol\u000a (mol glucose)(-1), whereas malate formation strongly decreased. Although\u000a fully aerobic conditions could be achieved, it was found that moderate\u000a oxygen limitation benefitted malate production. In conclusion, malic\u000a acid production with the engineered S. cerevisiae strain could be\u000a successfully transferred from shake flasks to 1-liter batch bioreactors\u000a by simultaneous optimization of four process parameters (pH and\u000a concentrations of CO(2), calcium, and O(2)). Under optimized conditions,\u000a a malate yield of 0.48 +/- 0.01 mol (mol glucose)(-1) was obtained in\u000a bioreactors, a 19% increase over yields in shake flask experiments.\u000aTC 2\u000aZ9 2\u000aSN 0099-2240\u000aUT WOS:000274017400015\u000aER\u000a\u000aPT J\u000aAU Abbott, Derek A.\u000a Zelle, Rintze M.\u000a Pronk, Jack T.\u000a van Maris, Antonius J. A.\u000aTI Metabolic engineering of Saccharomyces cerevisiae for production of\u000a carboxylic acids: current status and challenges\u000aSO FEMS YEAST RESEARCH\u000aVL 9\u000aIS 8\u000aBP 1123\u000aEP 1136\u000aDI 10.1111/j.1567-1364.2009.00537.x\u000aPD DEC 2009\u000aPY 2009\u000aAB To meet the demands of future generations for chemicals and energy and\u000a to reduce the environmental footprint of the chemical industry,\u000a alternatives for petrochemistry are required. Microbial conversion of\u000a renewable feedstocks has a huge potential for cleaner, sustainable\u000a industrial production of fuels and chemicals. Microbial production of\u000a organic acids is a promising approach for production of chemical\u000a building blocks that can replace their petrochemically derived\u000a equivalents. Although Saccharomyces cerevisiae does not naturally\u000a produce organic acids in large quantities, its robustness, pH tolerance,\u000a simple nutrient requirements and long history as an industrial workhorse\u000a make it an excellent candidate biocatalyst for such processes. Genetic\u000a engineering, along with evolution and selection, has been successfully\u000a used to divert carbon from ethanol, the natural endproduct of S.\u000a cerevisiae, to pyruvate. Further engineering, which included expression\u000a of heterologous enzymes and transporters, yielded strains capable of\u000a producing lactate and malate from pyruvate. Besides these metabolic\u000a engineering strategies, this review discusses the impact of transport\u000a and energetics as well as the tolerance towards these organic acids. In\u000a addition to recent progress in engineering S. cerevisiae for organic\u000a acid production, the key limitations and challenges are discussed in the\u000a context of sustainable industrial production of organic acids from\u000a renewable feedstocks.\u000aTC 11\u000aZ9 11\u000aSN 1567-1356\u000aUT WOS:000271264400001\u000aER\u000a\u000aPT J\u000aAU Zelle, Rintze M.\u000a de Hulster, Erik\u000a van Winden, WoUter A.\u000a de Waard, Pieter\u000a Dijkema, Cor\u000a Winkler, Aaron A.\u000a Geertman, Jan-Maarten A.\u000a van Dijken, Johannes P.\u000a Pronk, Jack T.\u000a van Maris, Antonius J. A.\u000aTI Malic acid production by Saccharomyces cerevisiae: Engineering of\u000a pyruvate carboxylation, oxaloacetate reduction, and malate export\u000aSO APPLIED AND ENVIRONMENTAL MICROBIOLOGY\u000aVL 74\u000aIS 9\u000aBP 2766\u000aEP 2777\u000aDI 10.1128/AEM.02591-07\u000aPD MAY 2008\u000aPY 2008\u000aAB Malic acid is a potential biomass-derivable \"building block\" for\u000a chemical synthesis. Since wild-type Saccharomyces cerevisiae strains\u000a produce only low levels of malate, metabolic engineering is required to\u000a achieve efficient malate production with this yeast. A promising pathway\u000a for malate production from glucose proceeds via carboxylation of\u000a pyruvate, followed by reduction of oxaloacetate to malate. This redox-\u000a and ATP-neutral, CO2-fixing pathway has a theoretical maximum yield of 2\u000a mol malate (mol glucose)(-1). A previously engineered glucose-tolerant,\u000a C-2-independent pyruvate decarboxylase-negative S. cerevisiae strain was\u000a used as the platform to evaluate the impact of individual and combined\u000a introduction of three genetic modifications: (i) overexpression of the\u000a native pyruvate carboxylase encoded by PYC2, (ii) high-level expression\u000a of an allele of the MDH3 gene, of which the encoded malate dehydrogenase\u000a was retargeted to the cytosol by deletion of the C-terminal peroxisomal\u000a targeting sequence, and (iii) functional expression of the\u000a Schizosaccharomyces pombe malate transporter gene SpMAE1. While single\u000a or double modifications improved malate production, the highest malate\u000a yields and titers were obtained with the simultaneous introduction of\u000a all three modifications. In glucose-grown batch cultures, the resulting\u000a engineered strain produced malate at titers of up to 59 g liter(-1) at a\u000a malate yield of 0.42 mol (mol glucose)(-1). Metabolic flux analysis\u000a showed that metabolite labeling patterns observed upon nuclear magnetic\u000a resonance analyses of cultures grown on C-13-labeled glucose were\u000a consistent with the envisaged nonoxidative, fermentative pathway for\u000a malate production. The engineered strains still produced substantial\u000a amounts of pyruvate, indicating that the pathway efficiency can be\u000a further improved.\u000aTC 15\u000aZ9 17\u000aSN 0099-2240\u000aUT WOS:000255567900024\u000aER\u000a\u000aEF",
|
||
"items": [
|
||
{
|
||
"itemType": "journalArticle",
|
||
"creators": [
|
||
{
|
||
"firstName": "Rintze M.",
|
||
"lastName": "Zelle",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jacob C.",
|
||
"lastName": "Harrison",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jack T.",
|
||
"lastName": "Pronk",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Antonius J. A.",
|
||
"lastName": "van Maris",
|
||
"creatorType": "author"
|
||
}
|
||
],
|
||
"notes": [],
|
||
"tags": [],
|
||
"seeAlso": [],
|
||
"attachments": [],
|
||
"extra": "WOS:000286597100004",
|
||
"title": "Anaplerotic Role for Cytosolic Malic Enzyme in Engineered Saccharomyces cerevisiae Strains",
|
||
"publicationTitle": "Applied and Environmental Microbiology",
|
||
"volume": "77",
|
||
"issue": "3",
|
||
"pages": "732-738",
|
||
"DOI": "10.1128/AEM.02132-10",
|
||
"date": "FEB 2011",
|
||
"abstractNote": "Malic enzyme catalyzes the reversible oxidative decarboxylation of malate to pyruvate and CO(2). The Saccharomyces cerevisiae MAE1 gene encodes a mitochondrial malic enzyme whose proposed physiological roles are related to the oxidative, malate-decarboxylating reaction. Hitherto, the inability of pyruvate carboxylase-negative (Pyc(-)) S. cerevisiae strains to grow on glucose suggested that Mae1p cannot act as a pyruvate-carboxylating, anaplerotic enzyme. In this study, relocation of malic enzyme to the cytosol and creation of thermodynamically favorable conditions for pyruvate carboxylation by metabolic engineering, process design, and adaptive evolution, enabled malic enzyme to act as the sole anaplerotic enzyme in S. cerevisiae. The Escherichia coli NADH-dependent sfcA malic enzyme was expressed in a Pyc(-) S. cerevisiae background. When PDC2, a transcriptional regulator of pyruvate decarboxylase genes, was deleted to increase intracellular pyruvate levels and cells were grown under a CO(2) atmosphere to favor carboxylation, adaptive evolution yielded a strain that grew on glucose (specific growth rate, 0.06 +/- 0.01 h(-1)). Growth of the evolved strain was enabled by a single point mutation (Asp336Gly) that switched the cofactor preference of E. coli malic enzyme from NADH to NADPH. Consistently, cytosolic relocalization of the native Mae1p, which can use both NADH and NADPH, in a pyc1,2 Delta pdc2 Delta strain grown under a CO(2) atmosphere, also enabled slow-growth on glucose. Although growth rates of these strains are still low, the higher ATP efficiency of carboxylation via malic enzyme, compared to the pyruvate carboxylase pathway, may contribute to metabolic engineering of S. cerevisiae for anaerobic, high-yield C(4)-dicarboxylic acid production.",
|
||
"ISSN": "0099-2240"
|
||
},
|
||
{
|
||
"itemType": "journalArticle",
|
||
"creators": [
|
||
{
|
||
"firstName": "Rintze M.",
|
||
"lastName": "Zelle",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Josh",
|
||
"lastName": "Trueheart",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jacob C.",
|
||
"lastName": "Harrison",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jack T.",
|
||
"lastName": "Pronk",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Antonius J. A.",
|
||
"lastName": "van Maris",
|
||
"creatorType": "author"
|
||
}
|
||
],
|
||
"notes": [],
|
||
"tags": [],
|
||
"seeAlso": [],
|
||
"attachments": [],
|
||
"extra": "WOS:000280633400006",
|
||
"title": "Phosphoenolpyruvate Carboxykinase as the Sole Anaplerotic Enzyme in Saccharomyces cerevisiae",
|
||
"publicationTitle": "Applied and Environmental Microbiology",
|
||
"volume": "76",
|
||
"issue": "16",
|
||
"pages": "5383-5389",
|
||
"DOI": "10.1128/AEM.01077-10",
|
||
"date": "AUG 2010",
|
||
"abstractNote": "Pyruvate carboxylase is the sole anaplerotic enzyme in glucose-grown cultures of wild-type Saccharomyces cerevisiae. Pyruvate carboxylase-negative (Pyc(-)) S. cerevisiae strains cannot grow on glucose unless media are supplemented with C(4) compounds, such as aspartic acid. In several succinate-producing prokaryotes, phosphoenolpyruvate carboxykinase (PEPCK) fulfills this anaplerotic role. However, the S. cerevisiae PEPCK encoded by PCK1 is repressed by glucose and is considered to have a purely decarboxylating and gluconeogenic function. This study investigates whether and under which conditions PEPCK can replace the anaplerotic function of pyruvate carboxylase in S. cerevisiae. Pyc(-) S. cerevisiae strains constitutively overexpressing the PEPCK either from S. cerevisiae or from Actinobacillus succinogenes did not grow on glucose as the sole carbon source. However, evolutionary engineering yielded mutants able to grow on glucose as the sole carbon source at a maximum specific growth rate of ca. 0.14 h(-1), one-half that of the (pyruvate carboxylase-positive) reference strain grown under the same conditions. Growth was dependent on high carbon dioxide concentrations, indicating that the reaction catalyzed by PEPCK operates near thermodynamic equilibrium. Analysis and reverse engineering of two independently evolved strains showed that single point mutations in pyruvate kinase, which competes with PEPCK for phosphoenolpyruvate, were sufficient to enable the use of PEPCK as the sole anaplerotic enzyme. The PEPCK reaction produces one ATP per carboxylation event, whereas the original route through pyruvate kinase and pyruvate carboxylase is ATP neutral. This increased ATP yield may prove crucial for engineering of efficient and low-cost anaerobic production of C(4) dicarboxylic acids in S. cerevisiae.",
|
||
"ISSN": "0099-2240"
|
||
},
|
||
{
|
||
"itemType": "journalArticle",
|
||
"creators": [
|
||
{
|
||
"firstName": "Rintze M.",
|
||
"lastName": "Zelle",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Erik",
|
||
"lastName": "De Hulster",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Wendy",
|
||
"lastName": "Kloezen",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jack T.",
|
||
"lastName": "Pronk",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Antonius J. A.",
|
||
"lastName": "van Maris",
|
||
"creatorType": "author"
|
||
}
|
||
],
|
||
"notes": [],
|
||
"tags": [],
|
||
"seeAlso": [],
|
||
"attachments": [],
|
||
"extra": "WOS:000274017400015",
|
||
"title": "Key Process Conditions for Production of C(4) Dicarboxylic Acids in Bioreactor Batch Cultures of an Engineered Saccharomyces cerevisiae Strain",
|
||
"publicationTitle": "Applied and Environmental Microbiology",
|
||
"volume": "76",
|
||
"issue": "3",
|
||
"pages": "744-750",
|
||
"DOI": "10.1128/AEM.02396-09",
|
||
"date": "FEB 2010",
|
||
"abstractNote": "A recent effort to improve malic acid production by Saccharomyces cerevisiae by means of metabolic engineering resulted in a strain that produced up to 59 g liter(-1) of malate at a yield of 0.42 mol (mol glucose)(-1) in calcium carbonate-buffered shake flask cultures. With shake flasks, process parameters that are important for scaling up this process cannot be controlled independently. In this study, growth and product formation by the engineered strain were studied in bioreactors in order to separately analyze the effects of pH, calcium, and carbon dioxide and oxygen availability. A near-neutral pH, which in shake flasks was achieved by adding CaCO(3), was required for efficient C(4) dicarboxylic acid production. Increased calcium concentrations, a side effect of CaCO(3) dissolution, had a small positive effect on malate formation. Carbon dioxide enrichment of the sparging gas (up to 15% [vol/vol]) improved production of both malate and succinate. At higher concentrations, succinate titers further increased, reaching 0.29 mol (mol glucose)(-1), whereas malate formation strongly decreased. Although fully aerobic conditions could be achieved, it was found that moderate oxygen limitation benefitted malate production. In conclusion, malic acid production with the engineered S. cerevisiae strain could be successfully transferred from shake flasks to 1-liter batch bioreactors by simultaneous optimization of four process parameters (pH and concentrations of CO(2), calcium, and O(2)). Under optimized conditions, a malate yield of 0.48 +/- 0.01 mol (mol glucose)(-1) was obtained in bioreactors, a 19% increase over yields in shake flask experiments.",
|
||
"ISSN": "0099-2240"
|
||
},
|
||
{
|
||
"itemType": "journalArticle",
|
||
"creators": [
|
||
{
|
||
"firstName": "Derek A.",
|
||
"lastName": "Abbott",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Rintze M.",
|
||
"lastName": "Zelle",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jack T.",
|
||
"lastName": "Pronk",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Antonius J. A.",
|
||
"lastName": "van Maris",
|
||
"creatorType": "author"
|
||
}
|
||
],
|
||
"notes": [],
|
||
"tags": [],
|
||
"seeAlso": [],
|
||
"attachments": [],
|
||
"extra": "WOS:000271264400001",
|
||
"title": "Metabolic engineering of Saccharomyces cerevisiae for production of carboxylic acids: current status and challenges",
|
||
"publicationTitle": "Fems Yeast Research",
|
||
"volume": "9",
|
||
"issue": "8",
|
||
"pages": "1123-1136",
|
||
"DOI": "10.1111/j.1567-1364.2009.00537.x",
|
||
"date": "DEC 2009",
|
||
"abstractNote": "To meet the demands of future generations for chemicals and energy and to reduce the environmental footprint of the chemical industry, alternatives for petrochemistry are required. Microbial conversion of renewable feedstocks has a huge potential for cleaner, sustainable industrial production of fuels and chemicals. Microbial production of organic acids is a promising approach for production of chemical building blocks that can replace their petrochemically derived equivalents. Although Saccharomyces cerevisiae does not naturally produce organic acids in large quantities, its robustness, pH tolerance, simple nutrient requirements and long history as an industrial workhorse make it an excellent candidate biocatalyst for such processes. Genetic engineering, along with evolution and selection, has been successfully used to divert carbon from ethanol, the natural endproduct of S. cerevisiae, to pyruvate. Further engineering, which included expression of heterologous enzymes and transporters, yielded strains capable of producing lactate and malate from pyruvate. Besides these metabolic engineering strategies, this review discusses the impact of transport and energetics as well as the tolerance towards these organic acids. In addition to recent progress in engineering S. cerevisiae for organic acid production, the key limitations and challenges are discussed in the context of sustainable industrial production of organic acids from renewable feedstocks.",
|
||
"ISSN": "1567-1356"
|
||
},
|
||
{
|
||
"itemType": "journalArticle",
|
||
"creators": [
|
||
{
|
||
"firstName": "Rintze M.",
|
||
"lastName": "Zelle",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Erik",
|
||
"lastName": "de Hulster",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "WoUter A.",
|
||
"lastName": "van Winden",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Pieter",
|
||
"lastName": "de Waard",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Cor",
|
||
"lastName": "Dijkema",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Aaron A.",
|
||
"lastName": "Winkler",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jan-Maarten A.",
|
||
"lastName": "Geertman",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Johannes P.",
|
||
"lastName": "van Dijken",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Jack T.",
|
||
"lastName": "Pronk",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "Antonius J. A.",
|
||
"lastName": "van Maris",
|
||
"creatorType": "author"
|
||
}
|
||
],
|
||
"notes": [],
|
||
"tags": [],
|
||
"seeAlso": [],
|
||
"attachments": [],
|
||
"extra": "WOS:000255567900024",
|
||
"title": "Malic acid production by Saccharomyces cerevisiae: Engineering of pyruvate carboxylation, oxaloacetate reduction, and malate export",
|
||
"publicationTitle": "Applied and Environmental Microbiology",
|
||
"volume": "74",
|
||
"issue": "9",
|
||
"pages": "2766-2777",
|
||
"DOI": "10.1128/AEM.02591-07",
|
||
"date": "MAY 2008",
|
||
"abstractNote": "Malic acid is a potential biomass-derivable \"building block\" for chemical synthesis. Since wild-type Saccharomyces cerevisiae strains produce only low levels of malate, metabolic engineering is required to achieve efficient malate production with this yeast. A promising pathway for malate production from glucose proceeds via carboxylation of pyruvate, followed by reduction of oxaloacetate to malate. This redox- and ATP-neutral, CO2-fixing pathway has a theoretical maximum yield of 2 mol malate (mol glucose)(-1). A previously engineered glucose-tolerant, C-2-independent pyruvate decarboxylase-negative S. cerevisiae strain was used as the platform to evaluate the impact of individual and combined introduction of three genetic modifications: (i) overexpression of the native pyruvate carboxylase encoded by PYC2, (ii) high-level expression of an allele of the MDH3 gene, of which the encoded malate dehydrogenase was retargeted to the cytosol by deletion of the C-terminal peroxisomal targeting sequence, and (iii) functional expression of the Schizosaccharomyces pombe malate transporter gene SpMAE1. While single or double modifications improved malate production, the highest malate yields and titers were obtained with the simultaneous introduction of all three modifications. In glucose-grown batch cultures, the resulting engineered strain produced malate at titers of up to 59 g liter(-1) at a malate yield of 0.42 mol (mol glucose)(-1). Metabolic flux analysis showed that metabolite labeling patterns observed upon nuclear magnetic resonance analyses of cultures grown on C-13-labeled glucose were consistent with the envisaged nonoxidative, fermentative pathway for malate production. The engineered strains still produced substantial amounts of pyruvate, indicating that the pathway efficiency can be further improved.",
|
||
"ISSN": "0099-2240"
|
||
}
|
||
]
|
||
},
|
||
{
|
||
"type": "import",
|
||
"input": "FN Thomson Reuters Web of Knowledge\u000aVR 1.0\u000aPT J\u000aAU Smith, L. J.\u000a Schwark, W. S.\u000a Cook, D. R.\u000a Moon, P. F.\u000a Erb, H. N.\u000a Looney, A. L.\u000aTI Pharmacokinetics of intravenous mivacurium in halothane-anesthetized\u000a dogs.\u000aSO Veterinary Surgery\u000aVL 27\u000aIS 2\u000aPS 170\u000aPY 1998\u000aUT CABI:19982209000\u000aDT Abstract only\u000aLA English\u000aSN 0161-3499\u000aCC LL900Animal Toxicology, Poisoning and Pharmacology (Discontinued March\u000a 2000); LL070Pets and Companion Animals\u000aCN 151-67-7\u000aDE anaesthesia; halothane; muscle relaxants; pharmacokinetics\u000aOR dogs\u000aBD Canis; Canidae; Fissipeda; carnivores; mammals; vertebrates; Chordata;\u000a animals; small mammals; eukaryotes\u000aER\u000a\u000aEF",
|
||
"items": [
|
||
{
|
||
"itemType": "journalArticle",
|
||
"creators": [
|
||
{
|
||
"firstName": "L. J.",
|
||
"lastName": "Smith",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "W. S.",
|
||
"lastName": "Schwark",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "D. R.",
|
||
"lastName": "Cook",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "P. F.",
|
||
"lastName": "Moon",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "H. N.",
|
||
"lastName": "Erb",
|
||
"creatorType": "author"
|
||
},
|
||
{
|
||
"firstName": "A. L.",
|
||
"lastName": "Looney",
|
||
"creatorType": "author"
|
||
}
|
||
],
|
||
"notes": [],
|
||
"tags": [
|
||
"anaesthesia",
|
||
"halothane",
|
||
"muscle relaxants",
|
||
"pharmacokinetics",
|
||
"dogs",
|
||
"Canis",
|
||
"Canidae",
|
||
"Fissipeda",
|
||
"carnivores",
|
||
"mammals",
|
||
"vertebrates",
|
||
"Chordata",
|
||
"animals",
|
||
"small mammals",
|
||
"eukaryotes"
|
||
],
|
||
"seeAlso": [],
|
||
"attachments": [],
|
||
"extra": "CABI:19982209000",
|
||
"title": "Pharmacokinetics of intravenous mivacurium in halothane-anesthetized dogs.",
|
||
"publicationTitle": "Veterinary Surgery",
|
||
"volume": "27",
|
||
"issue": "2",
|
||
"date": "1998",
|
||
"language": "English",
|
||
"ISSN": "0161-3499"
|
||
}
|
||
]
|
||
},
|
||
{
|
||
"type": "import",
|
||
"input": "FN Thomson Reuters Web of Knowledge\u000aVR 1.0\u000aPT J\u000aAU Smith, JM \u000aAF Smith, J. Mark\u000aTI Gripewater\u000aSO FIDDLEHEAD\u000aLA English \u000aDT Poetry\u000aNR 0\u000aTC 0\u000aZ9 0\u000aPU UNIV NEW BRUNSWICK\u000aPI FREDERICTON\u000aPA DEPT ENGLISH, CAMPUS HOUSE, PO BOX 4400, FREDERICTON, NB E3B 5A3, CANADA\u000aSN 0015-0630\u000aJ9 FIDDLEHEAD\u000aJI Fiddlehead\u000aPD SPR\u000aPY 2011\u000aIS 247\u000aBP 82\u000aEP 82\u000aPG 1\u000aWC Literary Reviews\u000aSC Literature\u000aGA 757VG\u000aUT WOS:000290115300030\u000aER\u000a\u000aEF",
|
||
"items": [
|
||
{
|
||
"itemType": "journalArticle",
|
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/** END TEST CASES **/
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