Threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli K 12. Reaction with 6-mercapto-9- -D-ribofuranosylpurine 5'-triphosphate
- PMID: 4326879
- DOI: 10.1021/bi00790a007
Threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli K 12. Reaction with 6-mercapto-9- -D-ribofuranosylpurine 5'-triphosphate
Similar articles
-
Homoserine dehydrogenase-aspartokinase of Escherichia coli. Comparison of threonine saturation and enzyme conformation.Biochemistry. 1971 Apr 27;10(9):1700-5. doi: 10.1021/bi00785a030. Biochemistry. 1971. PMID: 4931751 No abstract available.
-
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Binding of threonine and of pyridine nucleotides: stoichiometry and optical effects.Eur J Biochem. 1969 Mar;8(1):128-38. doi: 10.1111/j.1432-1033.1969.tb00505.x. Eur J Biochem. 1969. PMID: 4388664 No abstract available.
-
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of the protein catalyzing the two activities.Eur J Biochem. 1968 Jun;5(1):73-80. doi: 10.1111/j.1432-1033.1968.tb00339.x. Eur J Biochem. 1968. PMID: 4873312 No abstract available.
-
Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I.CRC Crit Rev Biochem. 1974;2(3):379-415. doi: 10.3109/10409237409105452. CRC Crit Rev Biochem. 1974. PMID: 4155358 Review. No abstract available.
-
Ligand-induced oligomerization and regulatory mechanism.CRC Crit Rev Biochem. 1974;2(3):343-78. doi: 10.3109/10409237409105451. CRC Crit Rev Biochem. 1974. PMID: 4374339 Review. No abstract available.
Cited by
-
Internal homologies in the two aspartokinase-homoserine dehydrogenases of Escherichia coli K-12.Proc Natl Acad Sci U S A. 1984 May;81(10):3019-23. doi: 10.1073/pnas.81.10.3019. Proc Natl Acad Sci U S A. 1984. PMID: 6374650 Free PMC article.