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2. Acetohydroxy acid synthase and threonine deaminase activities, and the biosynthesis of isoleucine-leucine-valine in Streptococcus bovis. Basso AL, Ricca E, Caruso C, Ferrara L, De Felice M. Res Microbiol; 1993 Sep; 144(7):539-45. PubMed ID: 8310179 [Abstract] [Full Text] [Related]
4. Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source. Dailey FE, Cronan JE. J Bacteriol; 1986 Feb; 165(2):453-60. PubMed ID: 3511034 [Abstract] [Full Text] [Related]
5. Suppressors of a genetic regulatory mutation affecting isoleucine-valine biosynthesis in Escherichia coli K-12. Hahn JE, Calhoun DH. J Bacteriol; 1978 Oct; 136(1):117-24. PubMed ID: 361682 [Abstract] [Full Text] [Related]
6. Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I. Belenky I, Steinmetz A, Vyazmensky M, Barak Z, Tittmann K, Chipman DM. FEBS J; 2012 Jun; 279(11):1967-79. PubMed ID: 22443469 [Abstract] [Full Text] [Related]
8. Synthesis of the isoleucyl- and valyl-tRNA synthetases and the isoleucine-valine biosynthetic enzymes in a threonine deaminase regulatory mutant of Escherichia coli K-12. Singer PA, Levinthal M, Williams LS. J Mol Biol; 1984 May 05; 175(1):39-55. PubMed ID: 6374157 [Abstract] [Full Text] [Related]
10. Valine 375 and phenylalanine 109 confer affinity and specificity for pyruvate as donor substrate in acetohydroxy acid synthase isozyme II from Escherichia coli. Steinmetz A, Vyazmensky M, Meyer D, Barak ZE, Golbik R, Chipman DM, Tittmann K. Biochemistry; 2010 Jun 29; 49(25):5188-99. PubMed ID: 20504042 [Abstract] [Full Text] [Related]
15. Allosteric regulation of biosynthetic threonine deaminase from Escherichia coli: effects of isoleucine and valine on active-site ligand binding and catalysis. Eisenstein E. Arch Biochem Biophys; 1995 Jan 10; 316(1):311-8. PubMed ID: 7840631 [Abstract] [Full Text] [Related]
16. An efficient approach to identify ilvA mutations reveals an amino-terminal catalytic domain in biosynthetic threonine deaminase from Escherichia coli. Fisher KE, Eisenstein E. J Bacteriol; 1993 Oct 10; 175(20):6605-13. PubMed ID: 8407838 [Abstract] [Full Text] [Related]