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Information on EC 4.2.1.40 - glucarate dehydratase and Organism(s) Pseudomonas putida and UniProt Accession P42206

for references in articles please use BRENDA:EC4.2.1.40
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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:
Pseudomonas putida
UNIPROT: P42206 not found.
Word Map
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucd, d-glucarate dehydratase, glucarate dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-Glucarate dehydratase
dehydratase, glucarate
-
-
-
0
GDH
-
-
-
0
GlucD
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O
show the reaction diagram
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
D-glucarate
3-deoxy-L-threo-2-hexulosarate
show the reaction diagram
D-glucarate
5-dehydro-4-deoxy-D-glucarate + H2O
show the reaction diagram
-
-
-
-
?
D-glucarate
D-idarate
show the reaction diagram
D-idarate
D-glucarate
show the reaction diagram
D-idarate
L-glucarate
show the reaction diagram
-
-
-
-
?
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
5-dehydro-4-deoxy-D-glucarate + H2O
show the reaction diagram
-
-
-
-
?
D-idarate
L-glucarate
show the reaction diagram
-
-
-
-
?
L-idarate
3-deoxy-L-threo-2-hexulosarate
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067 - 0.65
D-glucarate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 17
D-glucarate
4 - 21
L-idarate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUDD_PSEPU
451
0
49572
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
sequence alignment
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.3 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Palmer, D.R.J.; Wieczorek, S.J.; Hubbard, B.K.; Mrachko, G.T.; Gerit, J.A.
Importance of mechanistic imperatives in enzyme-catalyzed beta-elimination reactions: stereochemical consequences of the dehydration reaction catalyzed by D-galactonate dehydratase from Escherichia coli and D-glucarate dehydratase from Pseudomonas putida
J. Am. Chem. Soc.
199
9580-9581
1997
Pseudomonas putida
-
Manually annotated by BRENDA team
Palmer, D.R.J.; Gerit, J.A.
Evolution of enzymatic activities: multiple pathways for generating and partitioning a common enolic intermediate by glucarate dehydratase from Pseudomonas putida
J. Am. Chem. Soc.
118
10323-10342
1996
Pseudomonas putida
-
Manually annotated by BRENDA team
Palmer, D.R.J.; Hubbard, B.K.; Gerit, J.A.
Evolution of enzymatic activities in the enolase superfamily: partitioning of reactive intermediates by (D)-glucarate dehydratase from Pseudomonas putida
Biochemistry
37
14350-14357
1998
Pseudomonas putida
Manually annotated by BRENDA team
Gulick, A.M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida
Biochemistry
37
14358-14368
1998
Pseudomonas putida (P42206), Pseudomonas putida
Manually annotated by BRENDA team
Tian, B.; Wallrapp, F.; Kalyanaraman, C.; Zhao, S.; Eriksson, L.A.; Jacobson, M.P.
Predicting enzyme-substrate specificity with QM/MM methods: a case study of the stereospecificity of D-glucarate dehydratase
Biochemistry
52
5511-5513
2013
Pseudomonas putida
Manually annotated by BRENDA team
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