BRENDA - Enzyme Database
show all sequences of 1.8.3.6

Farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis

Huizinga, D.H.; Denton, R.; Koehler, K.G.; Tomasello, A.; Wood, L.; Sen, S.E.; Crowell, D.N.; Mol. Plant 3, 143-155 (2010)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Spodoptera frugiperda (Sf9) cells; gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
Arabidopsis thaliana
Engineering
Protein Variants
Commentary
Organism
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
Arabidopsis thaliana
Inhibitors
Inhibitors
Commentary
Organism
Structure
(2E,6E)-farnesal
-
Arabidopsis thaliana
diphenyl iodonium
-
Arabidopsis thaliana
diphenyl iodonium chloride
-
Arabidopsis thaliana
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)
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
Arabidopsis thaliana
N-acetyl-S-farnesyl-L-cysteine
-
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition; unlabeled S-farnesyl-L-cysteine effectively competes with [1-3H]-S-farnesyl-L-cysteine
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
-
Arabidopsis thaliana
S-farnesyl-L-homocysteine
-
Arabidopsis thaliana
S-geranyl-L-cysteine
-
Arabidopsis thaliana
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.045
-
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Arabidopsis thaliana
16020
-
microsome
-
Arabidopsis thaliana
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
55300
-
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
67000
-
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
Arabidopsis thaliana
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
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
Arabidopsis thaliana
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Arabidopsis thaliana
P57681
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
N-glycosylated; the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
Arabidopsis thaliana
proteolytic modification
proteolytically processed at the amino terminus
Arabidopsis thaliana
Reaction
Reaction
Commentary
Organism
Reaction ID
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2
kinetics and catalytic mechanism, overview
Arabidopsis thaliana
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seedling
-
Arabidopsis thaliana
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
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
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
no activity towards S-geranylgeranyl-L-cysteine
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
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
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
Synonyms
Synonyms
Commentary
Organism
farnesylcysteine lyase
-
Arabidopsis thaliana
FC lyase
-
Arabidopsis thaliana
FCLY
-
Arabidopsis thaliana
S-farnesyl-L-cysteine lyase
-
Arabidopsis thaliana
S-farnesyl-L-cysteine oxidase
-
Arabidopsis thaliana
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Arabidopsis thaliana
37
-
assay at
Arabidopsis thaliana
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
7.5
-
assay at
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Arabidopsis thaliana
Cofactor
Cofactor
Commentary
Organism
Structure
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
Arabidopsis thaliana
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.05
-
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
0.124
-
diphenyl iodonium chloride
pH 7.5, 30°C
Arabidopsis thaliana
0.187
-
S-farnesyl-L-homocysteine
pH 7.5, 30°C
Arabidopsis thaliana
0.194
-
S-geranyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
0.512
-
N-acetyl-S-farnesyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.05
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
(2E,6E)-farnesal
0.124
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
diphenyl iodonium
0.187
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
0.194
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
S-geranyl-L-cysteine
0.512
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Spodoptera frugiperda (Sf9) cells; gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Arabidopsis thaliana
Engineering (protein specific)
Protein Variants
Commentary
Organism
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
Arabidopsis thaliana
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.05
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
(2E,6E)-farnesal
0.124
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
diphenyl iodonium
0.187
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
0.194
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
S-geranyl-L-cysteine
0.512
-
recombinant enzyme, pH 7.5, 30°C
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(2E,6E)-farnesal
-
Arabidopsis thaliana
diphenyl iodonium
-
Arabidopsis thaliana
diphenyl iodonium chloride
-
Arabidopsis thaliana
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)
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
Arabidopsis thaliana
N-acetyl-S-farnesyl-L-cysteine
-
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition; unlabeled S-farnesyl-L-cysteine effectively competes with [1-3H]-S-farnesyl-L-cysteine
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
-
Arabidopsis thaliana
S-farnesyl-L-homocysteine
-
Arabidopsis thaliana
S-geranyl-L-cysteine
-
Arabidopsis thaliana
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.05
-
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
0.124
-
diphenyl iodonium chloride
pH 7.5, 30°C
Arabidopsis thaliana
0.187
-
S-farnesyl-L-homocysteine
pH 7.5, 30°C
Arabidopsis thaliana
0.194
-
S-geranyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
0.512
-
N-acetyl-S-farnesyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.045
-
S-(2E,6E)-farnesyl-L-cysteine
pH 7.5, 30°C
Arabidopsis thaliana
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Arabidopsis thaliana
16020
-
microsome
-
Arabidopsis thaliana
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
55300
-
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
67000
-
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
Arabidopsis thaliana
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
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
Arabidopsis thaliana
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
N-glycosylated; the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
Arabidopsis thaliana
proteolytic modification
proteolytically processed at the amino terminus
Arabidopsis thaliana
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seedling
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
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
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
no activity towards S-geranylgeranyl-L-cysteine
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
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
710018
Arabidopsis thaliana
(2E,6E)-farnesal + L-cysteine + H2O2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
Arabidopsis thaliana
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Arabidopsis thaliana
37
-
assay at
Arabidopsis thaliana
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
7.5
-
assay at
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Arabidopsis thaliana
General Information
General Information
Commentary
Organism
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
Arabidopsis thaliana
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
Arabidopsis thaliana
physiological function
the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
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
Arabidopsis thaliana
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
Arabidopsis thaliana
physiological function
the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine
Arabidopsis thaliana
Other publictions for EC 1.8.3.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
710018
Huizinga
Farnesylcysteine lyase is invo ...
Arabidopsis thaliana
Mol. Plant
3
143-155
2010
-
-
1
-
1
-
10
1
2
-
3
2
-
2
-
2
-
1
-
1
-
-
4
1
6
2
1
-
-
1
-
-
1
5
-
5
-
-
1
1
-
1
-
5
10
5
1
2
-
3
2
-
-
2
-
-
1
-
-
4
1
2
1
-
-
1
-
-
-
-
3
3
-
-
-
710279
Crowell
Arabidopsis thaliana plants po ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Plant J.
50
839-847
2007
-
-
1
-
1
-
2
-
1
-
-
2
-
5
-
-
-
-
-
6
-
-
6
-
4
1
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
1
-
-
2
-
-
1
-
-
2
-
-
-
-
-
6
-
-
6
-
1
-
-
-
2
-
-
-
-
3
3
-
-
-