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Enzyme Nomenclature
Information on EC 1.8.3.6 - farnesylcysteine lyase
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The expected taxonomic range for this enzyme is: Arabidopsis thaliana
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EC NUMBER 
COMMENTARY 
1.8.3.6
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RECOMMENDED NAME
GeneOntology No.
farnesylcysteine lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2
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S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2
kinetics and catalytic mechanism, overview
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
fcly mutants of Arabidopsis exhibit reduced S-farnesyl-L-cysteine lyase activity and an enhanced response to abscisic acid; S-(2E,6E)-farnesyl-L-cysteine accumulates in fcly mutants, leading to competitive inhibition of isoprenylcysteine methyltransferase activity, which show enhanced response to abscisic acid reversable by isoprenylcysteine methyltransferase overexpression. The abscisic acid hypersensitive phenotype of fcly plants is the result of farnesyl-L-cysteine accumulation and inhibition of isoprenylcysteine methyltransferase
malfunction
T-DNA insertions into the FCLY gene cause significant decreases in FC lyase activity and an enhanced response to abscisic acid in seed germination assays. The effects of FCLY mutations on abscisic acid sensitivity are even greater in the presence of exogenous farnesyl-L-cysteine
malfunction
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T-DNA insertions into the FCLY gene cause significant decreases in FC lyase activity and an enhanced response to abscisic acid in seed germination assays. The effects of FCLY mutations on abscisic acid sensitivity are even greater in the presence of exogenous farnesyl-L-cysteine
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metabolism
farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis. The enzyme is part of an recycling pathway in plants whereby the farnesal product od S-farnesyl-L-cysteine lyase is reduced to farnesol, which is subsequently phosphorylated to farnesyl diphosphate
metabolism
the enzyme is involved in the salvage cycle for S-(2E,6E)-farnesyl diphosphate in plants, overview
physiological function
the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine
physiological function
Arabidopsis FC lyase recognizes amide-linked S-(2E,6E)-farnesyl-L-cysteine and may have a role in deprenylation of farnesylated proteins
physiological function
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Arabidopsis FC lyase recognizes amide-linked S-(2E,6E)-farnesyl-L-cysteine and may have a role in deprenylation of farnesylated proteins
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
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-
?
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis. The enzyme is part of an recycling pathway in plants whereby the farnesal product od S-farnesyl-L-cysteine lyase is reduced to farnesol, which is subsequently phosphorylated to farnesyl diphosphate
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
no activity towards S-geranylgeranyl-L-cysteine
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
the enzyme is specific for S-farnesyl-L-cysteine. No activity towards S-geranyl-L-cysteine or S-geranylgeranyl-L-cysteine
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine, mechanism of action of Arabidopsis FC lyase, its dependence on FAD and molecular oxygen, overview
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
the enzyme is specific for S-farnesyl-L-cysteine. No activity towards S-geranyl-L-cysteine or S-geranylgeranyl-L-cysteine
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-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
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-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
P57681
farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis. The enzyme is part of an recycling pathway in plants whereby the farnesal product od S-farnesyl-L-cysteine lyase is reduced to farnesol, which is subsequently phosphorylated to farnesyl diphosphate
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition; unlabeled S-farnesyl-L-cysteine effectively competes with [1-3H]-S-farnesyl-L-cysteine
N-acetyl-S-farnesyl-L-cysteine
a 50fold molar excess of unlabeled N-acetyl-S-farnesyl-L-cysteine inhibits the conversion of [1-3H]-S-farnesyl-L-cysteine to [1-3H]-farnesal by more than 50%
additional information
no inhibition by S-geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine; no inhibition, S-geranylgeranyl-L-cysteine (0.325 mM), S-neryl-L-cysteine (0.5 mM), S-citronellyl-L-cysteine (0.5 mM), S-benzyl-L-cysteine (0.5 mM)
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additional information
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S-geranyl-L-cysteine or S-geranylgeranyl-L-cysteine fail to inhibit S-farnesyl-L-cysteine lyase
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additional information
S-geranyl-L-cysteine or S-geranylgeranyl-L-cysteine fail to inhibit S-farnesyl-L-cysteine lyase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
ubiquitously expressed in Arabidopsis tissues and organs
additional information
-
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
additional information
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
To generate the fcly-1:ICMTox and fcly-2:ICMTox lines, fcly-1 and fcly-2 mutants of Arabidopsis thaliana are transformed with a recombinant binary vector pCL108 containing the CaMV 35S promoter and the AtSTE14B coding sequence. Agrobacterium tumefaciens strain GV3101/pMP90 and the floral dip method are used for plant transformation
additional information
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T-DNA insertions mutants fcly-1 and fcly-2 plants exhibit reduced FCLY mRNA levels, as determined by semi-quantitative RT-PCR, and reduced FC lyase activity compared with Columbia (Col-0) and wild-type siblings. Significantly, germination of fcly-1 and fcly-2 seeds is inhibited by exogenous ABA at concentrations that did not affect wild-type Col-0 seeds
additional information
T-DNA insertions mutants fcly-1 and fcly-2 plants exhibit reduced FCLY mRNA levels, as determined by semi-quantitative RT-PCR, and reduced FC lyase activity compared with Columbia (Col-0) and wild-type siblings. Significantly, germination of fcly-1 and fcly-2 seeds is inhibited by exogenous ABA at concentrations that did not affect wild-type Col-0 seeds
additional information
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T-DNA insertions mutants fcly-1 and fcly-2 plants exhibit reduced FCLY mRNA levels, as determined by semi-quantitative RT-PCR, and reduced FC lyase activity compared with Columbia (Col-0) and wild-type siblings. Significantly, germination of fcly-1 and fcly-2 seeds is inhibited by exogenous ABA at concentrations that did not affect wild-type Col-0 seeds
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.3.6)
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