BRENDA - Enzyme Database show
show all sequences of 1.8.3.5

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)
Commentary
Organism
gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
Arabidopsis thaliana
Engineering
Amino acid exchange
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
diphenyl iodonium
-
Arabidopsis thaliana
additional information
no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition
Arabidopsis thaliana
S-(2E,6E)-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, 30C
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
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
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
P57681
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
Arabidopsis thaliana
Reaction
Reaction
Commentary
Organism
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
kinetics and catalytic mechanism, overview
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
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
required for activity, FC lyase is a flavoprotein
Arabidopsis thaliana
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.05
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-cysteine
0.124
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
diphenyl iodonium
0.187
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
0.194
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
S-geranyl-L-cysteine
0.512
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Cloned(Commentary) (protein specific)
Commentary
Organism
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
required for activity, FC lyase is a flavoprotein
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
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, 30C
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-cysteine
0.124
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
diphenyl iodonium
0.187
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
0.194
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
S-geranyl-L-cysteine
0.512
-
recombinant enzyme, pH 7.5, 30C
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
diphenyl iodonium
-
Arabidopsis thaliana
additional information
no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine
Arabidopsis thaliana
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition
Arabidopsis thaliana
S-(2E,6E)-farnesyl-L-homocysteine
-
Arabidopsis thaliana
S-geranyl-L-cysteine
-
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, 30C
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
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
the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
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
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
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
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
physiological function
the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine
Arabidopsis thaliana
Other publictions for EC 1.8.3.5
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
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)
743865
Dashty
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1
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1
1
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-
-
1
-
1
-
6
1
2
-
3
1
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2
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1
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1
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2
1
1
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1
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1
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5
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1
1
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1
-
5
6
-
1
2
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3
1
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1
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2
1
1
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1
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2
2
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706670
Banfi
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Homo sapiens
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1344-1352
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1
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2
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1
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1
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1
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1
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1
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1
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1
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1
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1
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1
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-
1
1
-
-
-
710279
Crowell
Arabidopsis thaliana plants po ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Plant J.
50
839-847
2007
-
-
1
-
1
-
-
-
1
-
-
2
-
5
-
-
-
-
-
1
-
-
4
-
1
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1
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1
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1
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1
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2
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1
-
-
4
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
667445
Wouters
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Mus musculus
Biochem. Biophys. Res. Commun.
346
491-500
2006
-
-
-
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3
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1
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3
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1
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3
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669763
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Bos taurus
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2
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1
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1
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3
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437708
Beigneux
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Mus musculus
J. Biol. Chem.
277
38358-38363
2002
-
-
1
-
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-
-
-
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1
-
4
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6
-
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4
-
1
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1
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1
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1
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6
-
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4
-
1
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1
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-
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-
437709
Digits
Stereospecificity and kinetic ...
Homo sapiens
J. Biol. Chem.
277
41086-41093
2002
-
-
-
-
-
-
2
2
-
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1
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2
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3
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1
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1
1
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1
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2
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1
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3
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