Cloned (Comment) | Organism |
---|---|
expressed in Spodoptera frugiperda (Sf9) cells | Arabidopsis thaliana |
gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system. | Arabidopsis thaliana |
Protein Variants | Comment | 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 | Comment | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.045 | - |
S-(2E,6E)-farnesyl-L-cysteine | pH 7.5, 30°C | Arabidopsis thaliana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Arabidopsis thaliana | 16020 | - |
microsome | - |
Arabidopsis thaliana | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | P57681 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | N-glycosylated | Arabidopsis thaliana |
glycoprotein | 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 | Comment | 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 | Comment | Organism | Textmining |
---|---|---|---|
seedling | - |
Arabidopsis thaliana | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O | no activity towards S-geranylgeranyl-L-cysteine | 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 | 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 | Arabidopsis thaliana | (2E,6E)-farnesal + L-cysteine + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE | Arabidopsis thaliana |
Synonyms | Comment | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Arabidopsis thaliana |
37 | - |
assay at | Arabidopsis thaliana |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Arabidopsis thaliana |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Arabidopsis thaliana |
Cofactor | Comment | 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% | Arabidopsis thaliana | |
FAD | required for activity, FC lyase is a flavoprotein | Arabidopsis thaliana |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | 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 Maximum | Comment | 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 |
General Information | Comment | Organism |
---|---|---|
malfunction | fcly mutants of Arabidopsis exhibit reduced S-farnesyl-L-cysteine lyase activity and an enhanced response to abscisic acid | Arabidopsis thaliana |
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 |
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 |