Information on EC 4.2.1.118 - 3-dehydroshikimate dehydratase

Word Map on EC 4.2.1.118
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:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.2.1.118
-
RECOMMENDED NAME
GeneOntology No.
3-dehydroshikimate dehydratase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-dehydro-shikimate = protocatechuate + H2O
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
petrobactin biosynthesis
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
quinate degradation I
-
-
quinate degradation II
-
-
shikimate degradation I
-
-
shikimate degradation II
-
-
quinate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
3-dehydroshikimate hydro-lyase
Catalyses an early step in the biosynthesis of petrobactin, a siderophore produced by many bacteria, including the human pathogen Bacillus anthracis. Requires divalent ions, with a preference for Mn2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9044-87-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 97-27
-
-
Manually annotated by BRENDA team
strain 97-27
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-3-dehydroshikimate
3,4-dihydroxybenzoate + H2O
show the reaction diagram
3-dehydroshikimate
protocatechuate + H2O
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-dehydroshikimate
protocatechuate + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activation
Mo2+
-
activation
additional information
-
a divalent metal ion is absolutely required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
-
decreases mDSD enzyme activity during purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125
(-)-3-dehydroshikimate
-
37C
0.00059 - 0.5
3-dehydroshikimate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.8
(-)-3-dehydroshikimate
Bacillus thuringiensis
-
37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
257
-
pH 7.5, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
less than 15% residual activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
-
minor component, and 5.0, minor component
5
-
major component, and 4.8, minor component
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultured in presence of shikimate
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36500
-
gel filtration
37000
-
SDS-PAGE
40367
-
x * 40367, calculated
76000
-
mDSD, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40367, calculated
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46
-
half-life 10 min
additional information
-
enzyme is sensitive to thermal denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
MgCl2 partially stabilizes the cytosolic isozyme during purification
-
the membrane-bound isozyme is stable in contrast to the cytosolic isoform
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, loss of 50% of activity within 3 days
-
0-2C, presence of 25 mM Mg2+, one week, less than 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native mDSD from strain IFO 3244 membrane fraction to homogeneity by solubilization with detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside, anion exchange and hydroxyapatite chromatography. The cytosolic isozyme sDSD is purified from the cytosolic fraction after centrifugation at 62000 x g followed by anion echange chromatograohy, ammonium sulfate precipitation, and dialysis, the enzyme activity is lost during dialysis
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Aspergillus nidulans
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complete loss of activity in presence of EDTA. More than 95% of activity can be restored in presence of Mg2+
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (137 entries)
Please use the Sequence Search for a specific query.