The Experts below are selected from a list of 138 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.
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.
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.
Christopher A. 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.
