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Information on EC 4.2.1.40 - glucarate dehydratase and Organism(s) Escherichia coli and UniProt Accession P0AES2

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.40 glucarate dehydratase
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0AES2 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
glucd, d-glucarate dehydratase, glucarate dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Glucarate dehydratase
-
-
-
-
dehydratase, glucarate
-
-
-
-
GDH
-
-
-
-
GlucD
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
D-glucarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9059-02-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-deoxy-4-fluoro-D-glucarate
?
show the reaction diagram
D-glucarate
3-deoxy-L-threo-2-hexulosarate + H2O
show the reaction diagram
L-idarate
3-deoxy-L-threo-2-hexulosarate
show the reaction diagram
D-glucarate
3-deoxy-L-threo-2-hexulosarate + H2O
show the reaction diagram
D-Glucarate
?
show the reaction diagram
-
first step in D-glucarate metabolism in bacteria
-
-
?
D-glucarate
D-idarate
show the reaction diagram
-
epimerization
epimerization
r
D-idarate
D-glucarate
show the reaction diagram
-
epimerization
epimerization
r
L-idarate
3-deoxy-L-threo-2-hexulosarate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Glucarate
?
show the reaction diagram
-
first step in D-glucarate metabolism in bacteria
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
located at the active site
Mn2+
-
less than one-third as effective as Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-deoxy-D-glucarate
-
xylarohydroxamate
-
Co2+
-
high concentrations
D-idaric acid
-
-
galactaric acid
-
-
Mn2+
-
high concentrations
p-chloromercuribenzene sulfonate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.8
D-glucarate
0.016
L-idarate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 44
4-deoxy-4-fluoro-D-glucarate
0.00033 - 35
D-glucarate
0.00025 - 35
L-idarate
20
D-glucarate
-
-
20
L-idarate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
Tris-maleate buffer
7.5
-
barbital buffer
7.5 - 8.5
-
Tris-HCl buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
sequence alignment
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D366A
reduced kcat for D-glucarate and L-idarate
D366N
reduced kcat for D-glucarate and 3fold reduced kcat for L-idarate
H339A
reduced kcat for D-glucarate and L-idarate
H339N
reduced kcat for D-glucarate and L-idarate
H339Q
reduced kcat for D-glucarate and L-idarate
K207Q
reduced kcat for D-glucarate and L-idarate
K207R
reduced kcat for D-glucarate and L-idarate
N341D
do not catalyze the dehydrofluorination of 4-deoxy-4-fluoro-D-glucarate
N341L
catalyzes the dehydrofluorination of 4-deoxy-4-fluoro-D-glucarate
Y150F
significant reduction of kcat for D-glucarate and L-idarate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
-
moderately stable
33840
7.5
-
most stable near
33840
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marsh, C.A.
An enzymatic determination of D-glucaric acid by conversion to pyruvate
Anal. Biochem.
145
266-272
1985
Escherichia coli
Manually annotated by BRENDA team
Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli
Biochemistry
37
14369-14375
1998
Bacillus subtilis, Escherichia coli, Pseudomonas putida
Manually annotated by BRENDA team
Blumenthal, H.J.
D-glucarate dehydratase
Methods Enzymol.
9
660-665
1966
Bacillus subtilis, Citrobacter freundii, Escherichia coli, Klebsiella aerogenes, Klebsiella pneumoniae, Paracolobactrum sp., Pectobacterium carotovorum, Priestia megaterium
-
Manually annotated by BRENDA team
Gulick, A.M.; Hubbard, B.K.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli
Biochemistry
39
4590-4602
2000
Escherichia coli (P0AES2), Escherichia coli
Manually annotated by BRENDA team
Gulick, A.M.; Hubbard, B.K.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli
Biochemistry
40
10054-10062
2001
Escherichia coli (P0AES2), Escherichia coli
Manually annotated by BRENDA team