Information on EC 4.2.1.163 - 2-oxo-hept-4-ene-1,7-dioate hydratase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
4.2.1.163
-
RECOMMENDED NAME
GeneOntology No.
2-oxo-hept-4-ene-1,7-dioate hydratase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(4Z)-2-oxohept-4-enedioate + H2O = (4S)-4-hydroxy-2-oxoheptanedioate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-hydroxyphenylacetate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(4S)-4-hydroxy-2-oxoheptanedioate hydro-lyase [(4Z)-2-oxohept-4-enedioate-forming]
Requires Mg2+ [2]. Part of a 4-hydroxyphenylacetate degradation pathway in Escherichia coli C.
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
(4Z)-2-oxohept-4-enedioate + H2O
(4S)-4-hydroxy-2-oxoheptanedioate
show the reaction diagram
2-hydroxy-2,4-heptadiene-1,7-dioate + H2O
?
show the reaction diagram
2-oxo-hept-4-ene-1,7-dioate + H2O
?
show the reaction diagram
additional information
?
-
the enzyme cannot process 2-oxo-3-heptene-1,7 dioate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(4Z)-2-oxohept-4-enedioate + H2O
(4S)-4-hydroxy-2-oxoheptanedioate
show the reaction diagram
2-hydroxy-2,4-heptadiene-1,7-dioate + H2O
?
show the reaction diagram
2-oxo-hept-4-ene-1,7-dioate + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
required for activity. The enzyme shows a slight preference for Mn2+ over Mg2+
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32500
-
x * 32500, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homopentamer
2 * 000, calculated from amino acid sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystals of the native and selenomethionine-labelled enzyme are grown at 0.1M MES (pH 6.0), 0.7 M potassium thiocyanate, 7% (w/v) PEG 12000, 5% (w/v) PEG 550 MME, 10 mM dithiothreitol and 0.1 M Tris (pH 7.0), 0.7 M potassium thiocyanate, 6.4% (w/v) PEG 20000, 7% (w/v) PEG 550 MME,10 mM dithiothreitol, respectively
sitting drop vapor diffusion method, using 6.4% (w/v) polyethylene glycol 20000, 5% (w/v) polyethylene glycol 550 monomethyl ether, 0.7 M potassium thiocyanate, in 50 mM MES pH 5.5
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HisTrap column chromatography, and Superdex 75 gel filtration
-
Q Sepharose column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) and B834(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-