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Information on EC 3.3.2.12 - oxepin-CoA hydrolase and Organism(s) Escherichia coli and UniProt Accession P77455

for references in articles please use BRENDA:EC3.3.2.12
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EC Tree
     3 Hydrolases
         3.3 Acting on ether bonds
             3.3.2 Ether hydrolases
                3.3.2.12 oxepin-CoA hydrolase
IUBMB Comments
The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 1.17.1.7, 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase.Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway [1,3,4]. The enzyme from Escherichia coli also exhibits enoyl-CoA hydratase activity utilizing crotonyl-CoA as a substrate .
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P77455
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
ECH-Aa, MaoC, oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+), paaZ, PaaZ-ECH, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ECH-Aa
246
-
oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (NADP+)
PaaZ-ECH
246
domain showing oxepin-CoA hydrolase activity
SYSTEMATIC NAME
IUBMB Comments
2-oxepin-2(3H)-ylideneacetyl-CoA hydrolyase
The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 1.17.1.7, 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase.Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway [1,3,4]. The enzyme from Escherichia coli also exhibits enoyl-CoA hydratase activity utilizing crotonyl-CoA as a substrate [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxepin-2(3H)-ylideneacetyl-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
show the reaction diagram
-
-
-
?
2-oxepin-2(3H)-ylideneacetyl-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
show the reaction diagram
-
addition of purified PaaZ enzyme to enzymatically produced epoxide and oxepin in the presence of PaaG protein leads to a complete NADP+-dependent conversion of epoxide and oxepin into 3-oxo-5,6-dehydrosuberyl-CoA. PaaZ functions as an oxepin-CoA hydrolase/3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase catalyzing the two-step conversion of the oxepin-CoA via the open-chain aldehyde intermediate to 3-oxo-5,6-dehydrosuberyl-CoA
-
-
?
crotonyl-CoA + H2O
(R)-3-hydroxybutyryl-CoA
show the reaction diagram
-
the enzyme shows 1% activity with crotonyl-CoA compared to oxepin-CoA
-
-
?
oxepin-CoA + H2O
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde
show the reaction diagram
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
oxepin-CoA
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
39
oxepin-CoA
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
metabolism
the paaZ gene product is responsible of the third enzymatic step in the aerobic catabolism of phenylacetate in Escherichia coli
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73045
x * 73045, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 73045, calculated from amino acid sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
amylose resin column chromatography
-
Ni2+-affinity column chromatography or amylose resin column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, S.J.; Lee, S.Y.
Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli
J. Bacteriol.
185
5391-5397
2003
Escherichia coli
Manually annotated by BRENDA team
Ismail, W.; El-Said Mohamed, M.; Wanner, B.; Datsenko, K.; Eisenreich, W.; Rohdich, F.; Bacher, A.; Fuchs, G.
Functional genomics by NMR spectroscopy: Phenylacetate catabolism in Escherichia coli
Eur. J. Biochem.
270
3047-3054
2003
Escherichia coli, Escherichia coli (P77455)
Manually annotated by BRENDA team
Ferrandez, A.; Minambres, B.; Garcia, B.; Olivera, E.; Luengo, J.; Garcia, J.; Diaz, E.
Catabolism of phenylacetic acid in Escherichia coli: Characterization of a new aerobic hybrid pathway
J. Biol. Chem.
273
25974-25986
1998
Escherichia coli, Escherichia coli (P77455), Escherichia coli W14
Manually annotated by BRENDA team
Teufel, R.; Gantert, C.; Voss, M.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
Studies on the mechanism of ring hydrolysis in phenylacetate degradation: A metabolic branching point
J. Biol. Chem.
286
11021-11034
2011
Escherichia coli
Manually annotated by BRENDA team
Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.
Bacterial phenylalanine and phenylacetate catabolic pathway revealed
Proc. Natl. Acad. Sci. USA
107
14390-14395
2010
Escherichia coli
Manually annotated by BRENDA team
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