These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
115 related articles for article (PubMed ID: 344323)
1. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of a unique cysteine induces a conformational change of the enzyme. Fontan E; Truffa-Bachi P J Biol Chem; 1978 Apr; 253(8):2758-62. PubMed ID: 344323 [No Abstract] [Full Text] [Related]
2. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of the enzyme: threonine binding and inhibition are functionally dissociable. Fontan E; Truffa-Bachi P J Biol Chem; 1978 Apr; 253(8):2754-7. PubMed ID: 344322 [TBL] [Abstract][Full Text] [Related]
3. Threonine inhibition of the aspartokinase--homoserine dehydrogenase I of Escherichia coli. A slow transient and cooperativity of inhibition of the aspartokinase activity. Bearer CF; Neet KE Biochemistry; 1978 Aug; 17(17):3523-30. PubMed ID: 28752 [No Abstract] [Full Text] [Related]
4. Threonine inhibition of the aspartokinase--homoserine dehydrogenase I of Escherichia coli. Stopped-flow kinetics and the cooperativity of inhibition of the homoserine dehydrogenase activity. Bearer CF; Neet KE Biochemistry; 1978 Aug; 17(17):3517-22. PubMed ID: 28751 [No Abstract] [Full Text] [Related]
5. Stepwise inactivation of Escherichia coli aspartokinase-homoserine dehydrogenase I. Müller K; Garel JR Biochemistry; 1984 Feb; 23(4):651-4. PubMed ID: 6370302 [TBL] [Abstract][Full Text] [Related]
6. Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Kinetic and spectroscopic effects upon binding of serine and threonine. Costrejean JM; Truffa-Bachi P J Biol Chem; 1977 Aug; 252(15):5332-6. PubMed ID: 328500 [TBL] [Abstract][Full Text] [Related]
7. Threonine inhibition of the aspartokinase--homoserine dehydrogenase I of Escherichia coli. Threonine binding studies. Bearer CF; Neet KE Biochemistry; 1978 Aug; 17(17):3512-6. PubMed ID: 28750 [TBL] [Abstract][Full Text] [Related]
8. The interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH. Müller K; Garel JR J Biol Chem; 1984 Feb; 259(4):2252-6. PubMed ID: 6365907 [TBL] [Abstract][Full Text] [Related]
10. Subunit structure of the methionine-repressible aspartokinase II--homoserine dehydrogenase II from Escherichia coli K12. Dautry-Varsat A; Sibilli-Weill L; Cohen GN Eur J Biochem; 1977 Jun; 76(1):1-6. PubMed ID: 328280 [TBL] [Abstract][Full Text] [Related]
11. Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment. Dautry-Varsat A; Cohen GN J Biol Chem; 1977 Nov; 252(21):7685-9. PubMed ID: 334767 [TBL] [Abstract][Full Text] [Related]
12. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K-12. Incubation of the enzyme in alkaline conditions: dissociation and disulfide-bridge formation. Jacques Y; Truffa-Bachi P Eur J Biochem; 1976 Mar; 62(3):485-90. PubMed ID: 4302 [TBL] [Abstract][Full Text] [Related]
13. Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E.coli K12. Veron M; Guillou Y; Cohen GN FEBS Lett; 1985 Feb; 181(2):381-4. PubMed ID: 2982665 [TBL] [Abstract][Full Text] [Related]
14. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I-Isolation and characterisation of the peptides produced by cyanogen bromide. Cossart-Gheerbrant P; Sibilli-Weill L; Briley PA; Chalvignac MA; Le Bras G; Cohen GN Biochim Biophys Acta; 1978 Aug; 535(2):206-15. PubMed ID: 354697 [TBL] [Abstract][Full Text] [Related]
15. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin. Briley PA; Sibilli L; Chalvignac MA; Cossart P; Le Bras G; De Wolf A; Cohen GN J Biol Chem; 1978 Dec; 253(24):8867-71. PubMed ID: 363710 [TBL] [Abstract][Full Text] [Related]
16. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Distribution of the methioninyl residues and of the cysteinyl and tryptophanyl tryptic peptides. Sibilli L; Cossart P; Chalvignac MA; Briley PA; Costrejean JM; Le Bras G; Cohen GN Biochimie; 1977; 59(11-12):943-6. PubMed ID: 343821 [No Abstract] [Full Text] [Related]
17. E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure. Belfaiza J; Fazel A; Müller K; Cohen GN Biochem Biophys Res Commun; 1984 Aug; 123(1):16-20. PubMed ID: 6383377 [TBL] [Abstract][Full Text] [Related]
18. Reversible dissociation of aspartokinase I/homoserine dehydrogenase I from Escherichia coli K 12. The active species is the tetramer. Veron M; Guillou Y; Fazel A; Cohen GN Eur J Biochem; 1985 Sep; 151(3):521-4. PubMed ID: 3896789 [TBL] [Abstract][Full Text] [Related]
19. Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 (lambda). Activation by monovalent cations and an analysis of the effect of the adenosine triphosphate-magnesium ion complex on this activation process. Ogilvie JW; Vickers LP; Clark RB; Jones MM J Biol Chem; 1975 Feb; 250(4):1242-50. PubMed ID: 163250 [TBL] [Abstract][Full Text] [Related]
20. A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers. Fazel A; Guillou Y; Cohen GN J Biol Chem; 1983 Nov; 258(22):13570-4. PubMed ID: 6315703 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]