Information on EC 1.1.1.B61 - shikimate dehydrogenase [NADP]+

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.B61
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
shikimate dehydrogenase [NADP]+
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-dehydroshikimate + NADPH + H+ = shikimate + NADP+
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
shikimate:NADP+ 3-oxidoreductase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
malfunction
-
a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate
metabolism
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and E.C. 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
show the reaction diagram
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
additional information
-
for Poptr5, no activity with shikimate is detectable in the presence of NAD+ even with elevated enzyme concentrations
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Epicatechin gallate
-
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epigallocatechin gallate
-
inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
additional information
-
screening for polyphenolc enzyme inhibitors, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.131
NADP+
-
pH 8.8, 22°C, with shikimate
0.223 - 0.685
shikimate
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
399
NADP+
-
pH 8.8, 22°C, with shikimate
428
shikimate
-
pH 8.8, 22°C, with NADP+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
Epicatechin gallate
Arabidopsis thaliana
-
pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
0.0021
epigallocatechin gallate
Arabidopsis thaliana
-
pH 8.8, 25°C, recombinant enzyme, AroE domain of the DQD-SDH enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
poplar DQD/SDHs have distinct expression profiles, organ-specific expression of poplar DQD/SDHs, overview
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
in solution
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB ID 2O7S
-
crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged DQD/SDH isozyme 5 from Escherichia coli strain M15 by nickel affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 CodonPlus by nickel affinity chromatography and dialysis
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 CodonPlus
-
recombinant His6-tagged DQD/SDH isozyme 5 overexpression in Escherichia coli strain M15
-