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Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+) and Organism(s) Aquifex aeolicus and UniProt Accession O67049

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EC Tree
IUBMB Comments
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)+].
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Aquifex aeolicus
UNIPROT: O67049
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The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shikimate dehydrogenase, skdh, sasdh, mtbsdh, shikimate 5-dehydrogenase, hpsdh, mtbsd, shikimate:nadp+ oxidoreductase, hi0607, tgsdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-dehydroshikimate reductase
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5-dehydroshikimic reductase
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dehydroshikimic reductase
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DHS reductase
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shikimate 5-dehydrogenase
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shikimate dehydrogenase
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shikimate oxidoreductase
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shikimate:NADP oxidoreductase
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shikimate:NADP+ 5-oxidoreductase
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shikimate:NADP+ oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
show the reaction diagram
the active enzyme for dehydrogenation of shikimate contains a deprotonated K70 residue, a deprotonated D106, and a protonated Y216. The hydride transfer and the deprotonation of the 3-hydroxyl group of shikimate proceed in a concerted manner. K70 functions as a general base and becomes protonated in the dehydrogenation reaction. The proton is then transferred to the bulk solvent via the short proton-conducting wire. D106 plays a critical role in the transfer of the proton to the bulk solvent
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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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)+].
CAS REGISTRY NUMBER
COMMENTARY hide
9026-87-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
dependent on
NADPH
dependent on
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0424
NADP+
0.0424 - 0.0425
shikimate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
55.5
NADP+
with shikimate, pH 9.0, 25°C
55 - 55.5
shikimate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes, the enzyme reaction represents the fourth step of the shikimate pathway
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme and in complex with both shikimate and NADP+, which assumes the closed conformation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli in native and His-tagged form
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gan, J.; Wu, Y.; Prabakaran, P.; Gu, Y.; Li, Y.; Andrykovitch, M.; Liu, H.; Gong, Y.; Yan, H.; Ji, X.
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism
Biochemistry
46
9513-9522
2007
Aquifex aeolicus (O67049), Aquifex aeolicus
Manually annotated by BRENDA team
Peek, J.; Christendat, D.
The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework
Arch. Biochem. Biophys.
566
85-99
2015
Aquifex aeolicus (O67049), Arabidopsis thaliana (Q9SQT8), Archaeoglobus fulgidus (O27957), Archaeoglobus fulgidus ATCC 49558 (O27957), Aspergillus nidulans (P07547), Aspergillus nidulans FGSC A4 (P07547), Corynebacterium glutamicum (A4QB65), Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Populus trichocarpa, Pseudomonas putida (Q88IJ7), Pseudomonas putida KT 2240 (Q88IJ7), Staphylococcus aureus, Staphylococcus epidermidis (Q5HNV1), Staphylococcus epidermidis ATCC 35984 (Q5HNV1), Toxoplasma gondii (Q6W3D0)
Manually annotated by BRENDA team