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

BRENDA support

Literature summary for 1.8.3.5 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
Search for more literature for 1.8.3.5

Cloned(Commentary)

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

Protein Variants

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

Inhibitors Comment 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 Comment Organism Structure
0.045
-
 S-(2E,6E)-farnesyl-L-cysteine pH 7.5, 30°C Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Arabidopsis thaliana 16020
-
microsome
-
 Arabidopsis thaliana
-
-

Molecular Weight [Da]

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Comment Textmining
Arabidopsis thaliana P57681
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites Arabidopsis thaliana

Reaction

Reaction Comment Organism Reaction ID
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2 kinetics and catalytic mechanism, overview Arabidopsis thaliana
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Synonyms

Synonyms Comment Organism
farnesylcysteine lyase
-
 Arabidopsis thaliana
FC lyase
-
 Arabidopsis thaliana
FCLY
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
FAD required for activity, FC lyase is a flavoprotein Arabidopsis thaliana

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.05
-
 recombinant enzyme, pH 7.5, 30°C Arabidopsis thaliana S-(2E,6E)-farnesyl-L-cysteine
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

General Information Comment 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