Information on EC 1.8.3.6 - farnesylcysteine lyase

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The expected taxonomic range for this enzyme is: Arabidopsis thaliana

EC NUMBER
COMMENTARY hide
1.8.3.6
-
RECOMMENDED NAME
GeneOntology No.
farnesylcysteine lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
farnesylcysteine salvage pathway
-
-
Terpenoid backbone biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
S-(2E,6E)-farnesyl-L-cysteine oxidase
A flavoprotein (FAD). In contrast to mammalian EC 1.8.3.5 (prenylcysteine oxidase) the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene FCLY
SwissProt
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
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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
FAD is tightly, but non-covalently, bound to S-farnesyl-L-cysteine lyase and is required for activity. The addition of excess FAD to the reaction enhances the S-farnesyl-L-cysteine lyase reaction by 30%; required for activity, FC lyase is a flavoprotein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E,6E)-farnesal
-
diphenyl iodonium
-
diphenyl iodonium chloride
-
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
N-acetyl-S-farnesyl-L-cysteine
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition; unlabeled S-farnesyl-L-cysteine effectively competes with [1-3H]-S-farnesyl-L-cysteine
S-(2E,6E)-farnesyl-L-homocysteine
-
S-farnesyl-L-homocysteine
-
S-geranyl-L-cysteine
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.124
diphenyl iodonium chloride
pH 7.5, 30°C
0.512
N-acetyl-S-farnesyl-L-cysteine
pH 7.5, 30°C
0.05
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30°C
0.187
S-farnesyl-L-homocysteine
pH 7.5, 30°C
0.194
S-geranyl-L-cysteine
pH 7.5, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
(2E,6E)-farnesal
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30°C
0.124
diphenyl iodonium
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30°C
0.512
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30°C
0.187
S-(2E,6E)-farnesyl-L-homocysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30°C
0.194
S-geranyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
ubiquitously expressed in Arabidopsis tissues and organs
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
55300
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
67000
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, 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
N-glycosylated; the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
proteolytic modification
proteolytically processed at the amino terminus
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Spodoptera frugiperda (Sf9) cells; gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
gene FCLY, encoded on chromosome 5, DNA and amino acid sequence determination and analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information