Information on EC 1.3.99.8 - 2-furoyl-CoA dehydrogenase

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The expected taxonomic range for this enzyme is: Pseudomonas putida

EC NUMBER
COMMENTARY hide
1.3.99.8
-
RECOMMENDED NAME
GeneOntology No.
2-furoyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-furoyl-CoA + H2O + acceptor = S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
5-hydroxymethylfurfural degradation
-
-
furfural degradation
-
-
Furfural degradation
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating)
A copper protein. The oxygen atom of the -OH produced is derived from water, not O2; the actual oxidative step is probably dehydrogenation of a hydrated form -CHOH-CH2- to -C(OH)=CH-, which tautomerizes non-enzymically to -CO-CH2-, giving (5-oxo-4,5-dihydro-2-furoyl)-CoA. Methylene blue, nitro blue, tetrazolium and a membrane fraction from Pseudomonas putida can act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-18-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain F2
-
-
Manually annotated by BRENDA team
strain Fu1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-furoyl-CoA + H2O + acceptor
S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor
show the reaction diagram
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
2-furoyl-CoA + H2O + acceptor
S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bactopterin
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
-
-
additional information
-
no Fe
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bathocuproin
-
-
Cuprizone
-
-
cyanide
tungstate
-
-
additional information
-
not inhibitory: diethyldithiocarbamate, p-chloromercuribenzoate, arsenite, iodoacetamide, 2-n-heptyl-4-hydroxyquinoline N-oxide, azide, alpha,alpha'-bipyridyl, Tiron (i.e. disodium 1,2-dihydroxybenzene-3,5-disulfonate), 8-hydroxyquinoline, menadione
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.05
2-Furoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.09
-
micromol 2-furoyl-CoA/min/mg, in crude extract
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
2-furoyl-CoA + nitro blue tetrazolium
8.5 - 9.5
-
2-furoyl-CoA + methylene blue
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
alpha2,beta2, 2 * 25000 + 2 * 55000, SDS-PAGE
55000
-
alpha2,beta2, 2 * 25000 + 2 * 55000, SDS-PAGE
100000
-
gel filtration
150000
-
PAGE, gel filtration
900000
-
gel filtration
3270000
-
sedimentation equilibrium
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable over a long period of time
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
single absorption peak at 273 nm
-