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GFO/IDH/MocA C-terminal domain
This entry includes the C-terminal domain found in a set of oxidorecuctases from GFO/IDH/MocA family, not included in Pfam:PF02894 [1-5]. Paper describing PDB structure 1evj. [1]. 11099381. Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation. Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN;. J Mol Biol. 2000;304:575-584. Paper describing PDB structure 1h6a. [2]. 11705375. Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands. Nurizzo D, Halbig D, Sprenger GA, Baker EN;. Biochemistry. 2001;40:13857-13867. Paper describing PDB structure 1ofg. [3]. 8994968. The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP. Kingston RL, Scopes RK, Baker EN;. Structure 1996;4:1413-1428. Paper describing PDB structure 2glx. [4]. 16906761. Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis. Dambe TR, Kuhn AM, Brossette T, Giffhorn F, Scheidig AJ;. Biochemistry. 2006;45:10030-10042. Paper describing PDB structure 2nvw. [5]. 17121853. Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p. Thoden JB, Sellick CA, Reece RJ, Holden HM;. J Biol Chem. 2007;282:1534-1538. (from Pfam)
Gfo/Idh/MocA family oxidoreductase
This family of enzymes utilise NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot. [1]. 8994968. The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP. Kingston RL, Scopes RK, Baker EN;. Structure 1996;4:1413-1428. (from Pfam)
inositol 2-dehydrogenase
inositol 2-dehydrogenase catalyzes the first step in inositol catabolism; it is involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose)
All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se.
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