Information on EC 1.8.3.5 - prenylcysteine oxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
1.8.3.5
-
RECOMMENDED NAME
GeneOntology No.
prenylcysteine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Terpenoid backbone biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
S-prenyl-L-cysteine:oxygen oxidoreductase
A flavoprotein (FAD). Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine. N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. May represent the final step in the degradation of prenylated proteins in mammalian tissues. Originally thought to be a simple lyase so it had been classified as EC 4.4.1.18.
CAS REGISTRY NUMBER
COMMENTARY hide
196717-99-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene FCLY
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
show the reaction diagram
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
show the reaction diagram
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
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
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphenyl iodonium
-
farnesal
-
non-competitive versus farnesyl-L-cysteine
Farnesol
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition
S-(2E,6E)-farnesyl-L-homocysteine
-
S-geranyl-L-cysteine
-
additional information
no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
farnesyl-L-cysteine
-
-
0.00069
farnesylcysteine
-
-
0.00084
geranylgeranylcysteine
-
-
0.05
O2
-
Km below
0.045
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000133
farnesyl-L-cysteine
Homo sapiens
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.124
diphenyl iodonium
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.512
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.05
S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.187
S-(2E,6E)-farnesyl-L-homocysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.194
S-geranyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.7
-
assay at, depending on type of assay
7.7
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
assay at
25
-
assay at
37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
VLDL contains a greater protein content of PCL1 than LDL or HDL
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55300
mass spectroscopy
63000
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene FCLY, encoded on chromosome 5, DNAS and amino acid sequence determination and analysis
gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information