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Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+) and Organism(s) Haemophilus influenzae and UniProt Accession P43876
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1.1.1.25 shikimate dehydrogenase (NADP+)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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Word Map
- 1.1.1.25
- 3-dehydroshikimate
- drug development
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subdural
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cinnamyl
- dahps
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5-enolpyruvylshikimate
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pentafunctional
- 3-dehydroquinase
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ammonialyase
- analysis
- diagnostics
- food industry
- agriculture
The taxonomic range for the selected organisms is: Haemophilus influenzae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shikimate dehydrogenase, skdh, sasdh, mtbsdh, shikimate 5-dehydrogenase, mtbsd, hpsdh, shikimate:nadp+ oxidoreductase, hi0607, tgsdh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
ORGANISM
UNIPROT
LITERATURE
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
conserved residues Asp103 and Lys67 are important for catalysis in all three paralogues, kinetic mechanism of paralogue HI0607 and substrate binding site
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
9026-87-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
quinate + NADP+
3-dehydroquinate + NADPH + H+
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reversible activity of YdiB, no activity with paralogue HI0607
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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analysis of the 3-dehydroshikimate binding site
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
quinate + NADP+
3-dehydroquinate + NADPH + H+
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reversible activity of YdiB, no activity with paralogue HI0607
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r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
binding site determinatiion and binding mode analysis, AroE contains a Rossmann fold NADPH binding domain
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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paralogue HI0607 is not affected by 5 mM of Zn2+, Ca2+, Mg2+, or Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
three-dimensional structure analysis of AroE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and selenomethionine-labeled enzyme, free and in complex with NADPH, sitting drop vapour diffusion method, 10 mg/m protein, with or without 5 mM NADPH, mixture in a ratio of 1:1 with crystallization solution containing 1.0 M sodium citrate, and 0.1 M 2-(cyclohexylamino)ethanesulfonic acid (CHES), pH 8.8, for the free enzyme, and 12% PEG 8000, 0.15 M calcium acetate, pH 7.8, and 0.1 M imidazole for the selenomethionine-labeled enzyme, 4°C, X-ray diffraction structure determination and analysis at 2.4 A and 1.95 A, respectively, structure modeling
catalytic domain with open twisted alpha/beta motif plus NADPH binding domain with typical Rossman fold
purified recombinant wild-type and selenomethionine-labeled paralogue HI0607, hanging drop vapour diffusion method, 0.001 ml protein solution containing 20 mg/ml protein mixed with equal volume of reservoir solution containing 0.1 M sodium acetate, pH 4.6, 2.0 M NaCl, and 10% v/v PEG 400, X-ray diffraction structure determination and analysis at 1.75 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D103X
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site-directed mutagenesis of paralogue HI0607, inactive mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain DL41
phylogenetic analysis of the three paralogues YdiB, AroE, and HI0607, DNA and amino acid sequence determination and analysis of paralogue HI0607, expression of wild-type paralogue HI0607 in Escherichia coli strain BL21(DE3) and of selenomethionine-labeled enzyme in strain B834(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ye, S.; Von Delft, F.; Brooun, A.; Knuth, M.W.; Swanson, R.V.; McRee, D.E.
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
J. Bacteriol.
185
4144-4151
2003
Haemophilus influenzae, Haemophilus influenzae (P43876)
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