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Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor.
Halgand F, Dumas R, Biou V, Andrieu JP, Thomazeau K, Gagnon J, Douce R, Forest E. Halgand F, et al. Among authors: biou v. Biochemistry. 1999 May 11;38(19):6025-34. doi: 10.1021/bi982412e. Biochemistry. 1999. PMID: 10320328
Moreover, crystallographic data for the enzyme-NADPH-Mg2+-IpOHA complex [Biou, V., et al. (1997) EMBO J. 16, 3405-3415] have shown that IpOHA was completely buried inside the active site. ...
Moreover, crystallographic data for the enzyme-NADPH-Mg2+-IpOHA complex [Biou, V., et al. (1997) EMBO J. 16, 3405-3415] have s …
A loop deletion in the plant acetohydroxy acid isomeroreductase homodimer generates an active monomer with reduced stability and altered magnesium affinity.
Wessel PM, Biou V, Douce R, Dumas R. Wessel PM, et al. Among authors: biou v. Biochemistry. 1998 Sep 15;37(37):12753-60. doi: 10.1021/bi980411g. Biochemistry. 1998. PMID: 9737852
Since the enzyme exhibits no kinetic cooperativity either for its cofactor (NADPH and magnesium) or for its substrates, the reason for dimerization of this enzyme was not obvious. Recently, crystallographic studies [Biou, V., et al. (1997) EMBO J. 16, 3405-3415] rev …
Since the enzyme exhibits no kinetic cooperativity either for its cofactor (NADPH and magnesium) or for its substrates, the reason for dimer …
Amino acid biosynthesis: new architectures in allosteric enzymes.
Curien G, Biou V, Mas-Droux C, Robert-Genthon M, Ferrer JL, Dumas R. Curien G, et al. Among authors: biou v. Plant Physiol Biochem. 2008 Mar;46(3):325-39. doi: 10.1016/j.plaphy.2007.12.006. Epub 2007 Dec 31. Plant Physiol Biochem. 2008. PMID: 18272376 Review.
42 results