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Effects of high pressure on the stability and activity of allosteric phosphoenolpyruvate carboxylase from Escherichia coli.

作者信息

Izui K

出版信息

J Biochem. 1973 Mar;73(3):505-13. doi: 10.1093/oxfordjournals.jbchem.a130109.

DOI:10.1093/oxfordjournals.jbchem.a130109
PMID:4579422
Abstract
摘要

相似文献

1
Effects of high pressure on the stability and activity of allosteric phosphoenolpyruvate carboxylase from Escherichia coli.
J Biochem. 1973 Mar;73(3):505-13. doi: 10.1093/oxfordjournals.jbchem.a130109.
2
Phosphoenolpyruvate carboxylase of Escherichia coli: alteration of allosteric properties by photooxidation.
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Phosphoenolpyruvate carboxylase of E. coli: discrimination of regulatory sites for four kinds of allosteric effectors by the method of genetic desensitization.
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Phosphoenolpyruvate carboxylase of Escherichia coli. Multiple conformational states elicited by allosteric effectors.
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Escherichia coli phosphoenolpyruvate carboxylase: competitive regulation by acetyl-coenzyme A and aspartate.
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Kinetic studies of acetyl coenzyme A activated phosphoenolpyruvate carboxylase: reverse effects with a fatty acid.
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Concerted regulation in vitro of phosphoenolpyruvate carboxylase from Escherichia coli.
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Studies of parameters affecting the allosteric nature of phosphoenolpyruvate carboxylase of Escherichia coli.
J Biol Chem. 1968 Jun 25;243(12):3517-25.
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Escherichia coli phosphoenolpyruvate carboxylase: studies on the mechanism of multiple allosteric interactions.大肠杆菌磷酸烯醇丙酮酸羧化酶：多重别构相互作用机制的研究
Arch Biochem Biophys. 1977 Oct;183(2):538-52. doi: 10.1016/0003-9861(77)90389-7.
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Kinetic studies on the allosteric nature of phosphoenolpyruvate carboxylase from Escherichia coli.
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