The Experts below are selected from a list of 144 Experts worldwide ranked by ideXlab platform
Shigeki Tsuchida - One of the best experts on this subject based on the ideXlab platform.
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Kinetic evaluation of β-neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin-converting enzyme
Biochimica et biophysica acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide beta-neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr1-Gly2-Gly3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of beta-neoendorphin1-7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of beta-neoendorphin1-9 to beta-neoendorphin1-7. The k(cat) values of the somatic Isozyme for beta-neoendorphin1-7 were 2-fold higher than those for beta-neoendorphin1-9, indicating that beta-neoendorphin1-7 is more rapidly hydrolyzed than beta-neoendorphin1-9. The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k(cat) values for beta-neoendorphin1-7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of beta-neoendorphin1-7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of beta-neoendorphin1-9 hydrolysis differed between the two Isozymes.
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kinetic evaluation of β neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin converting enzyme
Biochimica et Biophysica Acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Abstract Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide β -neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr 1 -Gly 2 -Gly 3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of β -neoendorphin 1–7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of β -neoendorphin 1–9 to β -neoendorphin 1–7 . The k cat values of the somatic Isozyme for β -neoendorphin 1–7 were 2-fold higher than those for β -neoendorphin 1–9 , indicating that β -neoendorphin 1–7 is more rapidly hydrolyzed than β -neoendorphin 1–9 . The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k cat values for β -neoendorphin 1–7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of β -neoendorphin 1–7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of β -neoendorphin 1–9 hydrolysis differed between the two Isozymes.
Makoto Hayakari - One of the best experts on this subject based on the ideXlab platform.
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Kinetic evaluation of β-neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin-converting enzyme
Biochimica et biophysica acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide beta-neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr1-Gly2-Gly3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of beta-neoendorphin1-7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of beta-neoendorphin1-9 to beta-neoendorphin1-7. The k(cat) values of the somatic Isozyme for beta-neoendorphin1-7 were 2-fold higher than those for beta-neoendorphin1-9, indicating that beta-neoendorphin1-7 is more rapidly hydrolyzed than beta-neoendorphin1-9. The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k(cat) values for beta-neoendorphin1-7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of beta-neoendorphin1-7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of beta-neoendorphin1-9 hydrolysis differed between the two Isozymes.
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kinetic evaluation of β neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin converting enzyme
Biochimica et Biophysica Acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Abstract Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide β -neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr 1 -Gly 2 -Gly 3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of β -neoendorphin 1–7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of β -neoendorphin 1–9 to β -neoendorphin 1–7 . The k cat values of the somatic Isozyme for β -neoendorphin 1–7 were 2-fold higher than those for β -neoendorphin 1–9 , indicating that β -neoendorphin 1–7 is more rapidly hydrolyzed than β -neoendorphin 1–9 . The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k cat values for β -neoendorphin 1–7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of β -neoendorphin 1–7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of β -neoendorphin 1–9 hydrolysis differed between the two Isozymes.
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.
Satoshi Murakami - One of the best experts on this subject based on the ideXlab platform.
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Kinetic evaluation of β-neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin-converting enzyme
Biochimica et biophysica acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide beta-neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr1-Gly2-Gly3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of beta-neoendorphin1-7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of beta-neoendorphin1-9 to beta-neoendorphin1-7. The k(cat) values of the somatic Isozyme for beta-neoendorphin1-7 were 2-fold higher than those for beta-neoendorphin1-9, indicating that beta-neoendorphin1-7 is more rapidly hydrolyzed than beta-neoendorphin1-9. The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k(cat) values for beta-neoendorphin1-7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of beta-neoendorphin1-7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of beta-neoendorphin1-9 hydrolysis differed between the two Isozymes.
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kinetic evaluation of β neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin converting enzyme
Biochimica et Biophysica Acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Abstract Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide β -neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr 1 -Gly 2 -Gly 3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of β -neoendorphin 1–7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of β -neoendorphin 1–9 to β -neoendorphin 1–7 . The k cat values of the somatic Isozyme for β -neoendorphin 1–7 were 2-fold higher than those for β -neoendorphin 1–9 , indicating that β -neoendorphin 1–7 is more rapidly hydrolyzed than β -neoendorphin 1–9 . The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k cat values for β -neoendorphin 1–7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of β -neoendorphin 1–7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of β -neoendorphin 1–9 hydrolysis differed between the two Isozymes.
Keizou Ookawa - One of the best experts on this subject based on the ideXlab platform.
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Kinetic evaluation of β-neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin-converting enzyme
Biochimica et biophysica acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide beta-neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr1-Gly2-Gly3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of beta-neoendorphin1-7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of beta-neoendorphin1-9 to beta-neoendorphin1-7. The k(cat) values of the somatic Isozyme for beta-neoendorphin1-7 were 2-fold higher than those for beta-neoendorphin1-9, indicating that beta-neoendorphin1-7 is more rapidly hydrolyzed than beta-neoendorphin1-9. The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k(cat) values for beta-neoendorphin1-7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of beta-neoendorphin1-7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of beta-neoendorphin1-9 hydrolysis differed between the two Isozymes.
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kinetic evaluation of β neoendorphin hydrolysis by the somatic and testicular Isozymes of human angiotensin converting enzyme
Biochimica et Biophysica Acta, 1997Co-Authors: Makoto Hayakari, Kimihiko Satoh, Keizou Ookawa, Hiroko Kano, Satoshi Murakami, Noriaki Ikeda, Shigeki TsuchidaAbstract:Abstract Angiotensin-converting enzyme (ACE) has both somatic and testicular Isozymes, the former possessing two catalytically active domains, amino-terminal and carboxyl-terminal, while the latter has only the carboxyl-terminal one. We compared hydrolysis processes of the nonapeptide β -neoendorphin by the two Isozymes of human ACE. Both Isozymes hydrolyzed the peptide to Tyr 1 -Gly 2 -Gly 3 by the sequential removal of carboxyl-terminal dipeptides in three consecutive steps. The rate constant values for the second step, conversion of β -neoendorphin 1–7 to Leu-enkephalin, by the somatic Isozyme in the presence of 10 or 200 mM NaCl were 4-fold higher than those for the first step, conversion of β -neoendorphin 1–9 to β -neoendorphin 1–7 . The k cat values of the somatic Isozyme for β -neoendorphin 1–7 were 2-fold higher than those for β -neoendorphin 1–9 , indicating that β -neoendorphin 1–7 is more rapidly hydrolyzed than β -neoendorphin 1–9 . The rate constant value for the second step at 10 mM NaCl was 5-fold higher than that for the testicular Isozyme. Similar extent of difference was also observed in k cat values for β -neoendorphin 1–7 between the two Isozymes. These results suggest that the amino-terminal domain of the somatic Isozyme mainly contributes to the conversion of β -neoendorphin 1–7 to Leu-enkephalin at a low NaCl concentration. Optimal chloride concentrations for the individual steps of β -neoendorphin 1–9 hydrolysis differed between the two Isozymes.
