1.8.3.6	malfunction	fcly mutants of Arabidopsis exhibit reduced S-farnesyl-L-cysteine lyase activity and an enhanced response to abscisic acid	710018	
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	710018	
1.8.3.6	malfunction	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	-, 710279	
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	710018	
1.8.3.6	metabolism	the enzyme is involved in the salvage cycle for S-(2E,6E)-farnesyl diphosphate in plants, overview	710279	
1.8.3.6	physiological function	Arabidopsis FC lyase recognizes amide-linked S-(2E,6E)-farnesyl-L-cysteine and may have a role in deprenylation of farnesylated proteins	-, 710279	
1.8.3.6	physiological function	the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine	710018