Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Huizinga, D.H.; Denton, R.; Koehler, K.G.; Tomasello, A.; Wood, L.; Sen, S.E.; Crowell, D.N.
    Farnesylcysteine lyase is involved in negative regulation of abscisic acid signaling in Arabidopsis (2010), Mol. Plant, 3, 143-155.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.5 gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system. Arabidopsis thaliana
1.8.3.6 expressed in Spodoptera frugiperda (Sf9) cells Arabidopsis thaliana
1.8.3.6 gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system. Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.5 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
1.8.3.6 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

EC Number Inhibitors Comment Organism Structure
1.8.3.5 diphenyl iodonium
-
 Arabidopsis thaliana
1.8.3.5 additional information no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine Arabidopsis thaliana
1.8.3.5 N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
 Arabidopsis thaliana
1.8.3.5 S-(2E,6E)-farnesyl-L-cysteine substrate inhibition Arabidopsis thaliana
1.8.3.5 S-(2E,6E)-farnesyl-L-homocysteine
-
 Arabidopsis thaliana
1.8.3.5 S-geranyl-L-cysteine
-
 Arabidopsis thaliana
1.8.3.6 (2E,6E)-farnesal
-
 Arabidopsis thaliana
1.8.3.6 diphenyl iodonium
-
 Arabidopsis thaliana
1.8.3.6 diphenyl iodonium chloride
-
 Arabidopsis thaliana
1.8.3.6 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
1.8.3.6 N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
 Arabidopsis thaliana
1.8.3.6 N-acetyl-S-farnesyl-L-cysteine
-
 Arabidopsis thaliana
1.8.3.6 S-(2E,6E)-farnesyl-L-cysteine substrate inhibition; unlabeled S-farnesyl-L-cysteine effectively competes with [1-3H]-S-farnesyl-L-cysteine Arabidopsis thaliana
1.8.3.6 S-(2E,6E)-farnesyl-L-homocysteine
-
 Arabidopsis thaliana
1.8.3.6 S-farnesyl-L-homocysteine
-
 Arabidopsis thaliana
1.8.3.6 S-geranyl-L-cysteine
-
 Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.5 0.045
-
 S-(2E,6E)-farnesyl-L-cysteine pH 7.5, 30°C Arabidopsis thaliana
1.8.3.6 0.045
-
 S-(2E,6E)-farnesyl-L-cysteine pH 7.5, 30°C Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.5 membrane
-
 Arabidopsis thaliana 16020
-
1.8.3.5 microsome
-
 Arabidopsis thaliana
-
-
1.8.3.6 membrane
-
 Arabidopsis thaliana 16020
-
1.8.3.6 microsome
-
 Arabidopsis thaliana
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.3.5 55000
-
 x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana
1.8.3.5 55300
-
 x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana
1.8.3.5 67000
-
 x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana
1.8.3.6 55000
-
 x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana
1.8.3.6 55300
-
 x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana
1.8.3.6 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.5 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
-
 ?
1.8.3.6 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
-
 ?
1.8.3.6 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

EC Number Organism UniProt Comment Textmining
1.8.3.5 Arabidopsis thaliana P57681
-
-
1.8.3.6 Arabidopsis thaliana P57681
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.8.3.5 glycoprotein the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites Arabidopsis thaliana
1.8.3.6 glycoprotein N-glycosylated Arabidopsis thaliana
1.8.3.6 glycoprotein the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites Arabidopsis thaliana
1.8.3.6 proteolytic modification proteolytically processed at the amino terminus Arabidopsis thaliana

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.3.5 an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2 kinetics and catalytic mechanism, overview Arabidopsis thaliana
a
1.8.3.6 S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O = (2E,6E)-farnesal + L-cysteine + H2O2 kinetics and catalytic mechanism, overview Arabidopsis thaliana
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.6 seedling
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.5 S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine Arabidopsis thaliana (2E,6E)-farnesal + L-cysteine + H2O2
-
 ?
1.8.3.5 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 Arabidopsis thaliana (2E,6E)-farnesal + L-cysteine + H2O2
-
 ?
1.8.3.6 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 Arabidopsis thaliana (2E,6E)-farnesal + L-cysteine + H2O2
-
 ?
1.8.3.6 S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O no activity towards S-geranylgeranyl-L-cysteine Arabidopsis thaliana (2E,6E)-farnesal + L-cysteine + H2O2
-
 ?
1.8.3.6 S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine Arabidopsis thaliana (2E,6E)-farnesal + L-cysteine + H2O2
-
 ?
1.8.3.6 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 Arabidopsis thaliana (2E,6E)-farnesal + L-cysteine + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.3.5 ? x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana
1.8.3.6 ? x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.8.3.5 farnesylcysteine lyase
-
 Arabidopsis thaliana
1.8.3.5 FC lyase
-
 Arabidopsis thaliana
1.8.3.5 FCLY
-
 Arabidopsis thaliana
1.8.3.6 farnesylcysteine lyase
-
 Arabidopsis thaliana
1.8.3.6 FC lyase
-
 Arabidopsis thaliana
1.8.3.6 FCLY
-
 Arabidopsis thaliana
1.8.3.6 S-farnesyl-L-cysteine lyase
-
 Arabidopsis thaliana
1.8.3.6 S-farnesyl-L-cysteine oxidase
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.3.5 30
-
 assay at Arabidopsis thaliana
1.8.3.6 30
-
 assay at Arabidopsis thaliana
1.8.3.6 37
-
 assay at Arabidopsis thaliana

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.8.3.6 7.5
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.3.5 7.5
-
 assay at Arabidopsis thaliana
1.8.3.6 7.5
-
 assay at Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.5 FAD required for activity, FC lyase is a flavoprotein Arabidopsis thaliana
1.8.3.6 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% Arabidopsis thaliana
1.8.3.6 FAD required for activity, FC lyase is a flavoprotein Arabidopsis thaliana

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.8.3.6 0.05
-
 S-(2E,6E)-farnesyl-L-cysteine pH 7.5, 30°C Arabidopsis thaliana
1.8.3.6 0.124
-
 diphenyl iodonium chloride pH 7.5, 30°C Arabidopsis thaliana
1.8.3.6 0.187
-
 S-farnesyl-L-homocysteine pH 7.5, 30°C Arabidopsis thaliana
1.8.3.6 0.194
-
 S-geranyl-L-cysteine pH 7.5, 30°C Arabidopsis thaliana
1.8.3.6 0.512
-
 N-acetyl-S-farnesyl-L-cysteine pH 7.5, 30°C Arabidopsis thaliana

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.8.3.5 0.05
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana S-(2E,6E)-farnesyl-L-cysteine
1.8.3.5 0.124
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana diphenyl iodonium
1.8.3.5 0.187
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana S-(2E,6E)-farnesyl-L-homocysteine
1.8.3.5 0.194
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana S-geranyl-L-cysteine
1.8.3.5 0.512
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
1.8.3.6 0.05
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana (2E,6E)-farnesal
1.8.3.6 0.124
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana diphenyl iodonium
1.8.3.6 0.187
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana S-(2E,6E)-farnesyl-L-homocysteine
1.8.3.6 0.194
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana S-geranyl-L-cysteine
1.8.3.6 0.512
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana N-acetyl-S-(2E,6E)-farnesyl-L-cysteine

General Information

EC Number General Information Comment Organism
1.8.3.5 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
1.8.3.5 physiological function the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine Arabidopsis thaliana
1.8.3.6 malfunction fcly mutants of Arabidopsis exhibit reduced S-farnesyl-L-cysteine lyase activity and an enhanced response to abscisic acid Arabidopsis thaliana
1.8.3.6 malfunction 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
1.8.3.6 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
1.8.3.6 physiological function the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine Arabidopsis thaliana