The Experts below are selected from a list of 165 Experts worldwide ranked by ideXlab platform
Aron W. Fenton - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Pyruvate Kinase From Thermoanaerobacterium saccharolyticum by IMP Is Independent of the Extra-C Domain.
Frontiers in microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogs generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
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inhibition of pyruvate kinase from thermoanaerobacterium saccharolyticum by IMP is independent of the extra c domain
Frontiers in Microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogues generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
Lee R Lynd - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Pyruvate Kinase From Thermoanaerobacterium saccharolyticum by IMP Is Independent of the Extra-C Domain.
Frontiers in microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogs generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
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inhibition of pyruvate kinase from thermoanaerobacterium saccharolyticum by IMP is independent of the extra c domain
Frontiers in Microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogues generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
Marybeth Maloney - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Pyruvate Kinase From Thermoanaerobacterium saccharolyticum by IMP Is Independent of the Extra-C Domain.
Frontiers in microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogs generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
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inhibition of pyruvate kinase from thermoanaerobacterium saccharolyticum by IMP is independent of the extra c domain
Frontiers in Microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogues generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
Daniel G. Olson - One of the best experts on this subject based on the ideXlab platform.
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Inhibition of Pyruvate Kinase From Thermoanaerobacterium saccharolyticum by IMP Is Independent of the Extra-C Domain.
Frontiers in microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogs generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
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inhibition of pyruvate kinase from thermoanaerobacterium saccharolyticum by IMP is independent of the extra c domain
Frontiers in Microbiology, 2021Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. FentonAbstract:The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for IMProved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogues generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
Jose Carlos Cameselle - One of the best experts on this subject based on the ideXlab platform.
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rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase i substrate specificities of mg2 and or mn2 dependent hydrolases acting on adp ribose
Biochimica et Biophysica Acta, 1995Co-Authors: Jose Canales, Rosa Maria Pinto, Maria Jesus Costas, Maria Teresa Hernandez, Asuncion Miro, Diego Bernet, Ascension Fernandez, Jose Carlos CameselleAbstract:Abstract Three rat liver nucleoside(5′) diphosphosugar (NDP-sugar) or nucleoside(5′) diphosphoalcohol pyrophosphatases are described: two were previously identified in experiments measuring Mg 2+ -dependent ADP-ribose pyrophosphatase activity (Miro et al. (1989) FEBS Lett. 244, 123–126), and the other is a new, Mn 2+ -dependent ADP-ribose pyrophosphatase. They are resolved by ion-exchange chromatography, and differ by their substrate and cation specificities, K M values for ADP-ribose, pH-activity profiles, molecular weights and isoelectric points. The enzymes were tested for activity towards: reducing (ADP-ribose, IDP-ribose) and non-reducing NDP-sugars (ADP-glucose, ADP-mannose, GDP-mannose, UDP-mannose, UDP-glucose, UDP-xylose, CDP-glucose), CDP-alcohols (CDP-glycerol, CDP-ethanolamine, CDP-choline), dinucleotides (diadenosine pyrophosphate, NADH, NAD + , FAD), nucleoside(5′) mono- and diphosphates (AMP, CMP, GMP, ADP, CDP) and dTMP p -nitrophenyl ester. Since the enzymes have not been purified to homogeneity, more than three pyrophosphatases may be present, but the co-purification of activities, thermal co-inactivation, and inhibition experiments give support to: (i) an ADP-ribose pyrophosphatase highly specific for ADP(IDP)-ribose in the presence of Mg 2+ , but active also on non-reducing ADP-hexoses and dinucleotides (not on NAD + ) when Mg 2+ was replaced with Mn 2+ ; (ii) a Mn 2+ -dependent pyrophosphatase active on ADP(IDP)-ribose, dinucleotides and CDP-alcohols; (iii) a rather unspecific pyrophosphatase that, with Mg 2+ , was active on AMP(IMP)-containing NDP-sugars and dinucleotides (not on NAD + ), and with Mn 2+ , was also active on non-adenine NDP-sugars and CDP-alcohols. The enzymes differ from nucleotide pyrophosphatase/phosphodiesterase-I (NPPase/PDEaseI) by their substrate specificities and by their cytosolic location and solubility in the absence of detergents. Although NPPase/PDEaseI is much more active in rat liver, its known location in the non-cytoplasmic sides of plasma and endoplasmic reticulum membranes, together with the known cytoplasmic synthesis of NDP-sugars and CDP-alcohols, permit the speculation that the pyrophosphatases studied in this work may have a cellular role.
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Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+- and/or Mn2+-dependent hydrolases acting on ADP-ribose☆
Biochimica et biophysica acta, 1995Co-Authors: Jose Canales, Rosa Maria Pinto, Maria Jesus Costas, Asuncion Miro, Diego Bernet, Ascension Fernandez, María Teresa Hernández, Jose Carlos CameselleAbstract:Abstract Three rat liver nucleoside(5′) diphosphosugar (NDP-sugar) or nucleoside(5′) diphosphoalcohol pyrophosphatases are described: two were previously identified in experiments measuring Mg 2+ -dependent ADP-ribose pyrophosphatase activity (Miro et al. (1989) FEBS Lett. 244, 123–126), and the other is a new, Mn 2+ -dependent ADP-ribose pyrophosphatase. They are resolved by ion-exchange chromatography, and differ by their substrate and cation specificities, K M values for ADP-ribose, pH-activity profiles, molecular weights and isoelectric points. The enzymes were tested for activity towards: reducing (ADP-ribose, IDP-ribose) and non-reducing NDP-sugars (ADP-glucose, ADP-mannose, GDP-mannose, UDP-mannose, UDP-glucose, UDP-xylose, CDP-glucose), CDP-alcohols (CDP-glycerol, CDP-ethanolamine, CDP-choline), dinucleotides (diadenosine pyrophosphate, NADH, NAD + , FAD), nucleoside(5′) mono- and diphosphates (AMP, CMP, GMP, ADP, CDP) and dTMP p -nitrophenyl ester. Since the enzymes have not been purified to homogeneity, more than three pyrophosphatases may be present, but the co-purification of activities, thermal co-inactivation, and inhibition experiments give support to: (i) an ADP-ribose pyrophosphatase highly specific for ADP(IDP)-ribose in the presence of Mg 2+ , but active also on non-reducing ADP-hexoses and dinucleotides (not on NAD + ) when Mg 2+ was replaced with Mn 2+ ; (ii) a Mn 2+ -dependent pyrophosphatase active on ADP(IDP)-ribose, dinucleotides and CDP-alcohols; (iii) a rather unspecific pyrophosphatase that, with Mg 2+ , was active on AMP(IMP)-containing NDP-sugars and dinucleotides (not on NAD + ), and with Mn 2+ , was also active on non-adenine NDP-sugars and CDP-alcohols. The enzymes differ from nucleotide pyrophosphatase/phosphodiesterase-I (NPPase/PDEaseI) by their substrate specificities and by their cytosolic location and solubility in the absence of detergents. Although NPPase/PDEaseI is much more active in rat liver, its known location in the non-cytoplasmic sides of plasma and endoplasmic reticulum membranes, together with the known cytoplasmic synthesis of NDP-sugars and CDP-alcohols, permit the speculation that the pyrophosphatases studied in this work may have a cellular role.