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Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+) and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58484
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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
-
subdural
-
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: Methanocaldococcus jannaschii
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, hpsdh, mtbsd, shikimate:nadp+ oxidoreductase, hi0607, tgsdh, 
more
topSYNONYM 
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
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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shikimate 5-dehydrogenase
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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
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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r
additional information
?
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fourth enzyme in the shikimate biosynthetic pathway
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-
?
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
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
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-
-
r
additional information
?
-
-
fourth enzyme in the shikimate biosynthetic pathway
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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dinucleotide cofactor binding domain structure is a Rossmann fold
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
additional information
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NADP+, compact alpha/beta sandwich with two domains for binding substrate and cofactor, resp.
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aroE, expression of GST-tagged SeMet-labeled enzyme in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Padyana, A.K.; Burley, S.K.
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution
Structure
11
1005-1013
2003
Methanocaldococcus jannaschii (Q58484), Methanocaldococcus jannaschii
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