This enzyme belongs to the superfamily of NAD(P)H-dependent shikimate dehydrogenase. This superfamily had been previously subdivided into four groups (1) AroE, EC=1.1.1.25, Shikimate dehydrogenases; (2) YdiB, EC=1.1.1.282, Shikimate/quinate dehydrogenases; (3) SdhL;EC=1.1.1.25, Shikimate dehydrogenase-like protein; (4) RifI, EC=1.1.1.25, Shikimate dehydrogenase (literature [12]). This enzyme corresponds to AroE. According to the literature [10], this enzyme catalyzes the following reversible reactions: (A) Hydride transfer from C5 of shikimate to nicotinamide of NADP+; Oxidation or dehydrogenation: (A0) Asp100 (of 2ev9) modulates the activity of Lys64 by its negative charge. (A1) Lys64 acts as a general base to deprotonate 5-hydoxyl group, whereas hydride transfer from C5 of shikimate to C4 of NADP+ occurs. (B) Hydride transfer from nicotinamide of NADPH to C5 of dehydroshikimate; Reduction: (B0) Asp100 (of 2ev9) modulates the activity of Lys64 by its negative charge. (B1) Lys64 acts as a general acid to protonate 5-carbonyl group, whereas hydride transfer from C4 of NADPH to C5 of dehydroshikimate occurs.
Leucine Dehydrogenase; Chain A, domain 1
Phenylalanine, tyrosine and tryptophan biosynthesis
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass.
The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase.
Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP.
The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, SUBUNIT.
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT. , X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, CATALYTIC ACTIVITY, SUBUNIT.
Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli.
Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 90-603 IN COMPLEX WITH SHIKIMATE AND TARTRATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-336; SER-338; LYS-385; ASP-423 AND TYR-550.
Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism.
1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum.
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.
X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase from Staphylococcus epidermidis.
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, MUTAGENESIS OF LYS-67 AND ASP-103, SUBUNIT.
Structural analysis of a set of proteins resulting from a bacterial genomics project.
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-288 IN COMPLEX WITH NAD.
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism.