Information on EC 1.3.1.28 - 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase

for references in articles please use BRENDA:EC1.3.1.28
Word Map on EC 1.3.1.28
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

top print hide
EC NUMBER
COMMENTARY hide
1.3.1.28
-
top print hide
RECOMMENDED NAME
GeneOntology No.
2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate + NADH + H+
show the reaction diagram
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,3-dihydroxybenzoate biosynthesis
-
-
enterobactin biosynthesis
-
-
Biosynthesis of siderophore group nonribosomal peptides
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
(2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase
-
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
37250-40-1
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JT strains
-
-
Manually annotated by BRENDA team
JT strains
-
-
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate + NAD+
2,3-dihydroxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
2-cyclohexen-1-ol + NAD+
1-oxo-2-cyclohexene + NADH
show the reaction diagram
-
-
-
r
3-hydroxy-4-cyclohexene-1-carboxylate
3-oxo-4-cyclohexene-1-carboxylate + NADH
show the reaction diagram
-
reversible only with 3-keto compounds, not with 2-keto compounds
-
r
4-isopropyl-2,3-dihydroxybenzoate + NAD+
?
show the reaction diagram
4-trifluoromethyl-2,3-dihydro-2,3-dihydroxybenzoate + NAD+
4-trifluoromethyl-2,3-dihydroxybenzoate + NADH
show the reaction diagram
cis-1,3-cyclohexadiene-5,6-diol + NAD+
?
show the reaction diagram
-
-
-
-
r
cis-3-hydroxy-cyclohexane-1-carboxylate + NAD+
3-oxo-cyclohexane-1-carboxylate + NADH
show the reaction diagram
-
-
-
r
methyl-2,3-dihydro-3-hydroxybenzoate + NAD+
3-hydroxybenzoate + NADH
show the reaction diagram
-
-
-
r
methyl-3-hydroxy-1,4-cyclohexadien-1-carboxylate + NAD+
3-hydroxybenzoate + NADH
show the reaction diagram
-
-
-
r
trans-1,3-cyclohexadiene-5,6-diol + NAD+
?
show the reaction diagram
-
-
-
-
r
trans-2,3-dihydro-2,3-dihydroxybenzoate + NAD+
2,3-dihydroxybenzoate + NADH
show the reaction diagram
trans-3-hydroxy-cyclohexane-1-carboxylate + NAD+
3-oxo-cyclohexane-1-carboxylate + NADH
show the reaction diagram
-
-
-
r
top print hide
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
(2S,3S)-2,3-dihydro-2,3-dihydroxybenzoate + NAD+
2,3-dihydroxybenzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Trifluoromethyl-2,3-dihydro-2,3-dihydroxybenzoate
-
competitive inhibition
cis-2-hydroxy-3-cyclohexen-1-carboxylate
-
-
cis-2-hydroxycyclohexane-1-carboxylate
-
-
trans-2-hydroxycyclohexane-1-carboxylate
-
-
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
2,3-Dihydro-2,3-dihydroxybenzoate
-
-
83.3
2-Cyclohexen-1-ol
-
-
0.017
4-isopropyl-2,3-dihydroxybenzoate
-
-
168
cis-3,5-cyclohexadiene-1,2-diol
-
-
2.8
cis-3-hydroxy-4-cyclohexene-1-carboxylate
-
-
4.1
cis-3-hydroxycyclohexane-1-carboxylic acid
-
-
0.26
methyl 2,3-dihydro-2,3-dihydroxybenzoate
-
-
1.7
methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate
-
-
0.037
NAD+
-
substrate 4-isopropyl-2,3-dihydroxybenzoate
16.5
trans-3,5-cyclohexadiene-1,2-diol
-
-
1.9
trans-3-hydroxy-2-cyclohexene-1-carboxylate
-
-
25.2
trans-3-hydroxycyclohexane-1-carboxylic acid
-
-
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25.3
2,3-dihydo-2,3-dihydroxybenzoate
-
-
1
2-Cyclohexen-1-ol
-
-
16.7
cis-3,5-cyclohexadiene-1,2-diol
-
-
23
cis-3-hydroxy-4-cyclohexene-1-carboxylate
-
-
5
cis-3-hydroxycyclohexane-1-carboxylic acid
-
-
17.5
methyl 2,3-dihydro-2,3-dihydroxybenzoate
-
-
3
methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate
-
-
92.5
trans-2,3-dihydro-2,3-dihydroxy-benzoate
-
-
1
trans-3,5-cyclohexadiene-1,2-diol
-
-
5
trans-3-hydroxy-2-cyclohexene-1-carboxylate
-
-
0.733
trans-3-hydroxycyclohexane-1-carboxylic acid
-
-
top print hide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
4-Trifluoromethyl-2,3-dihydro-2,3-dihydroxybenzoate
-
-
1.4
cis-2-hydroxy-3-cyclohexen-1-carboxylate
-
-
3.3
cis-2-hydroxycyclohexane-1-carboxylate
-
-
2.3
trans-2-hydroxycyclohexane-1-carboxylate
-
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0046
-
enzyme activity in crude extracts of cells grown in the presence of 0.002 mM iron, enzyme is repressed by high iron concentrations
top print hide
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
-
x * 26000, deduced from nucleotide sequence
210000
-
gel filtration
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 26000, deduced from nucleotide sequence
octamer
-
8 * 26249-26253, deduced from nucleotide sequence
tetramer
additional information
-
enzyme can form a specific complex with 2,3-dihydroxybenzoate-AMP ligase EntE. Cross-linked product with a molecular mass of more than 250 kDa, suggesting a complex stoichiometry of one EntA tetramer and four EntE monomers. Addition of a 4-fold excess of EntA to an EntE assay mixture results in a 6fold stimulation of EntE activity; enzyme undergoes concentration-dependent dimer-tetramer self-association with a KD value of 12.3 microM, analytical ultracentrifugation
top print hide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.0 A resolution by hanging-drop method
-
top print hide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable after chromatography on DEAE cellulose
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by two IMAC chromatography steps
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into vector pET15b and expressed in Escherichia coli BL21(DE3)
-
top
Show AA Sequence (862 entries)
Please use the Sequence Search for a specific query.
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.28)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)