Protein Family Models

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)

Date:

2024-08-14

Date:

2024-08-14

This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389. [1]. 9126843. Crystal structure of a ternary complex of D-2-hydroxyisocaproate. dehydrogenase from Lactobacillus casei, NAD+ and. 2-oxoisocaproate at 1.9 A resolution.. Dengler U, Niefind K, Kiess M, Schomburg D;. J Mol Biol 1997;267:640-660. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Date:

2023-01-04

This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704).

Gene:

ahcY

Date:

2023-01-04