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Information on EC 4.2.1.42 - galactarate dehydratase and Organism(s) Oceanobacillus iheyensis and UniProt Accession Q8EMJ9

for references in articles please use BRENDA:EC4.2.1.42
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.42 galactarate dehydratase
IUBMB Comments
The enzyme from the bacterium Escherichia coli is specific for galactarate , while the enzyme from Salmonella typhimurium also has activity with L-talarate (cf. EC 4.2.1.156, L-talarate dehydratase) . cf. EC 4.2.1.158, galactarate dehydratase (D-threo-forming).
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This record set is specific for:
Oceanobacillus iheyensis
UNIPROT: Q8EMJ9
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Word Map
The taxonomic range for the selected organisms is: Oceanobacillus iheyensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
galactarate dehydratase, a9cg74, stm3697, l-talarate/galactarate dehydratase, galrd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Dehydratase, galactarate
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-
-
-
Galactarate dehydrase
-
-
-
-
galactarate dehydratase
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-
GalcD
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
The enzyme from the bacterium Escherichia coli is specific for galactarate [2], while the enzyme from Salmonella typhimurium also has activity with L-talarate (cf. EC 4.2.1.156, L-talarate dehydratase) [3]. cf. EC 4.2.1.158, galactarate dehydratase (D-threo-forming).
CAS REGISTRY NUMBER
COMMENTARY hide
37290-78-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
galactarate
5-dehydro-4-deoxy D-glucarate + H2O
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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structure contains two Mg2+ ions located 10.4 A from one another, with one located in the canonical position in the (beta/alpha)7beta-barrel domain, the second is located in a site within the capping domain
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.62 - 4.4
galactarate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013 - 6.8
galactarate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00029 - 11
galactarate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H45Q
-
has no detectable activity
R162N
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retains a small amount of activity
Y164F
-
has no detectable activity
Y90F
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is catalytically impaired. Structure of the mutant in complex with Mg2+ and galactarate has a well-defined C-terminal segment through residue 387, well-ordered electron density for galactarate, and Mg2+ ions in both metal sites for both protomers comprising the asymmetric unit
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by centrifugation, sonication, on Ni-NTA column and by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into a TOPO vector (pSGX3), and transformed into Escherichia coli TOP10 competent cells. Gene in the pSGX3 vector transformed into Escherichia coli strains XL1-Blue for transformation and BL21(DE3) for expression
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rakus, J.F.; Kalyanaraman, C.; Fedorov, A.A.; Fedorov, E.V.; Mills-Groninger, F.P.; Toro, R.; Bonanno, J.; Bain, K.; Sauder, J.M.; Burley, S.K.; Almo, S.C.; Jacobson, M.P.; Gerlt, J.A.
Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis
Biochemistry
48
11546-11558
2009
Oceanobacillus iheyensis
Manually annotated by BRENDA team