Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
Acetohydroxy acid isomeroreductase, NADPH-binding domain
Acetohydroxy acid isomeroreductase catalyses the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, Pfam:PF01450. [1]. 9218783. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E;. EMBO J 1997;16:3405-3415. [2]. 16322583. The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG;. Protein Sci. 2005;14:3089-3100. [3]. 19362563. Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures. Leung EW, Guddat LW;. J Mol Biol. 2009;389:167-182. (from Pfam)
Acetohydroxy acid isomeroreductase, catalytic domain
Acetohydroxy acid isomeroreductase catalyses the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. [1]. 9218783. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E;. EMBO J 1997;16:3405-3415. (from Pfam)
NADP-dependent ketol-acid reductoisomerase
NADP-dependent ketol-acid reductoisomerase catalyzes the conversion of 2-(S)-acetolactate (2SAL) into (R)-dihydroxyisovalerate (RDHIV), the second step in the biosynthesis of the branched-chain amino acids (BCAAs) valine, leucine and isoleucine
ketol-acid reductoisomerase
Ketol-acid reductoisomerase is the second enzyme in the parallel isoleucine-valine biosynthetic pathway. Nearly all members of this family are designated EC 1.1.1.86, meaning specificity for NADPH, but a rare few are noted to be specific for NADH (EC 1.1.1.382) or for either (EC 1.1.1.383).
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on