Leucine Dehydrogenase; Chain A, domain 1
Phenylalanine, tyrosine and tryptophan biosynthesis
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, SUBUNIT.
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 (1.50 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT. , X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, CATALYTIC ACTIVITY, SUBUNIT.
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.
Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, MUTAGENESIS OF LYS-67 AND ASP-103, SUBUNIT.
Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae.
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-288 IN COMPLEX WITH NAD.
Structural analysis of a set of proteins resulting from a bacterial genomics project.
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.
Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway.
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism.
Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism.
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.
1.6 angstroms structure of an NAD+-dependent quinate dehydrogenase from Corynebacterium glutamicum.
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.
X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase from Staphylococcus epidermidis.
Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP.
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.