Information on EC 4.2.1.158 - galactarate dehydratase (D-threo-forming)

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

EC NUMBER
COMMENTARY hide
4.2.1.158
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RECOMMENDED NAME
GeneOntology No.
galactarate dehydratase (D-threo-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
galactarate = (2S,3R)-2,3-dihydroxy-5-oxohexanedioate + H2O
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
galactarate hydro-lyase (3-deoxy-D-threo-hex-2-ulosarate-forming)
The enzyme has been characterized from the bacterium Oceanobacillus iheyensis. cf. EC 4.2.1.42, galactarate dehydratase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
galactarate
2-oxo-D-threo-4,5-dihydroxyadipate + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
structure contains two Mg2+ ions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.62
galactarate
pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.8
galactarate
pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
galactarate
pH 8.0, 30°C
PDB
SCOP
CATH
ORGANISM
UNIPROT
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant Y90F. A Tyr 164-Arg 162 dyad is the base that initiates the reaction by abstraction of the alpha-proton and Tyr 90 is the acid that facilitates departure of the beta-OH leaving group. The 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, the second is located in a site within the capping domain
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y90F
catalytically impaired