A flavoprotein (FAD). In contrast to mammalian EC 1.8.3.5 (prenylcysteine oxidase) the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine.
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The expected taxonomic range for this enzyme is: Arabidopsis thaliana
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SYSTEMATIC NAME
IUBMB Comments
S-(2E,6E)-farnesyl-L-cysteine oxidase
A flavoprotein (FAD). In contrast to mammalian EC 1.8.3.5 (prenylcysteine oxidase) the farnesylcysteine lyase from Arabidopsis is specific for S-farnesyl-L-cysteine and shows no activity with S-geranylgeranyl-L-cysteine.
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
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
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
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
a 50fold molar excess of unlabeled N-acetyl-S-farnesyl-L-cysteine inhibits the conversion of [1-3H]-S-farnesyl-L-cysteine to [1-3H]-farnesal by more than 50%
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
T-DNA insertions into the FCLY gene cause significant decreases in FC lyase activity and an enhanced response to abscisic acid in seed germination assays. The effects of FCLY mutations on abscisic acid sensitivity are even greater in the presence of exogenous farnesyl-L-cysteine
T-DNA insertions into the FCLY gene cause significant decreases in FC lyase activity and an enhanced response to abscisic acid in seed germination assays. The effects of FCLY mutations on abscisic acid sensitivity are even greater in the presence of exogenous farnesyl-L-cysteine
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
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
T-DNA insertions mutants fcly-1 and fcly-2 plants exhibit reduced FCLY mRNA levels, as determined by semi-quantitative RT-PCR, and reduced FC lyase activity compared with Columbia (Col-0) and wild-type siblings. Significantly, germination of fcly-1 and fcly-2 seeds is inhibited by exogenous ABA at concentrations that did not affect wild-type Col-0 seeds
T-DNA insertions mutants fcly-1 and fcly-2 plants exhibit reduced FCLY mRNA levels, as determined by semi-quantitative RT-PCR, and reduced FC lyase activity compared with Columbia (Col-0) and wild-type siblings. Significantly, germination of fcly-1 and fcly-2 seeds is inhibited by exogenous ABA at concentrations that did not affect wild-type Col-0 seeds
T-DNA insertions mutants fcly-1 and fcly-2 plants exhibit reduced FCLY mRNA levels, as determined by semi-quantitative RT-PCR, and reduced FC lyase activity compared with Columbia (Col-0) and wild-type siblings. Significantly, germination of fcly-1 and fcly-2 seeds is inhibited by exogenous ABA at concentrations that did not affect wild-type Col-0 seeds
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1.8.3.6 farnesylcysteine lyase
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