NAD+ cannot replace NADP+ . In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase . cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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SYSTEMATIC NAME
IUBMB Comments
shikimate:NADP+ 3-oxidoreductase
NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
the structure reveals an enzyme with a deep cleft, which contains the active site, formed at the junction of two domains. The C-terminal domain is easily recognizable as a Rossmann fold dinucleotide binding domain, responsible for binding the NADP cofactor. The N-terminal substrate binding and dimerization domain, an alpha-beta-alpha sandwich, represents a unique topological fold, structure modeling
purified recombinant AroE bound to cofactor NADP+, hanging drop vapour diffusion method at 25°C, 10 mg/ml protein in 20 mM HEPES, pH 7.1, and 0.1 M KCl, is mixed with reservoir solution containing 20 mM HEPES, pH 7.1, 20% PEG 3350, and 0.2 M ammonium fluoride, cryoprotection with 15% glycerol, X-ray diffraction structure determination and analysis at 2.35 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged SeMet-labeled enzyme from Escherichia coli strain BL21 by glutathione affinity and ion exchange chromatography, proteolytic removal of the GST-tag