Information on EC 4.2.1.156 - L-talarate dehydratase

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The expected taxonomic range for this enzyme is: Salmonella enterica subsp. enterica serovar Typhimurium

EC NUMBER
COMMENTARY hide
4.2.1.156
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RECOMMENDED NAME
GeneOntology No.
L-talarate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-altarate = 5-dehydro-4-deoxy-D-glucarate + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-altarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
Requires Mg2+. The enzyme, isolated from the bacteria Salmonella typhimurium and Polaromonas sp. JS666, also has activity with galactarate (cf. EC 4.2.1.42, galactarate dehydratase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional L-talarate/galactarate dehydratase, activites of ECs 4.2.1.42 and 4.2.1.156
SwissProt
Manually annotated by BRENDA team
bifunctional L-talarate/galactarate dehydratase, activites of ECs 4.2.1.42 and 4.2.1.156
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-talarate
5-dehydro-4-deoxy-D-glucarate + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required. Ligands are residues Asp226, Glu252, and Glu278
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
L-talarate
Salmonella enterica subsp. enterica serovar Typhimurium
Q8ZL58
pH 8.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.1
L-talarate
Salmonella enterica subsp. enterica serovar Typhimurium
Q8ZL58
pH 8.0, 25°C
140261
PDB
SCOP
CATH
ORGANISM
UNIPROT
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structures of the wild type enzyme complexed with L-lyxarohydroxamate, and of the K197A mutant complexed with L-glucarate. Residue Lys 197 functions as the galactarate-specific base and His 328 functions as the L-talarate-specific base
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H328A
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
H328N
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
K197A
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
H328N
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inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
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K197A
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inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate
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