Information on EC 1.8.3.5 - prenylcysteine oxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.8.3.5
-
RECOMMENDED NAME
GeneOntology No.
prenylcysteine oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
show the reaction diagram
-
-
-
-
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
show the reaction diagram
kinetics and catalytic mechanism, overview
P57681
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Terpenoid backbone biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
S-prenyl-L-cysteine:oxygen oxidoreductase
A flavoprotein (FAD). Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine. N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. May represent the final step in the degradation of prenylated proteins in mammalian tissues. Originally thought to be a simple lyase so it had been classified as EC 4.4.1.18.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 4.4.1.18
-
-
formerly
-
farnesylcysteine lyase
P57681
-
FC lyase
P57681
-
FC lyase
Arabidopsis thaliana Col-0
P57681
-
-
FCLY
P57681
gene name
FCLY
Arabidopsis thaliana Col-0
P57681
gene name
-
flavin adenine dinucleotide (FAD)-dependent thioether oxidase
-
-
PCL
-
-
PCL1
Q9UHG3
-
PCLY
-
-
-
-
prenylcysteine lyase
-
-
-
-
prenylcysteine lyase
-
-
prenylcysteine lyase
Q9UHG3
-
prenylcysteine oxidase1
Q99JK4
-
CAS REGISTRY NUMBER
COMMENTARY
196717-99-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene FCLY
SwissProt
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
gene FCLY
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mouse, wild type and knockout mutants
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
P57681
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
malfunction
-, P57681
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 acidsensitivity are even greater in the presence of exogenous S-(2E,6E)-farnesyl-L-cysteine
malfunction
Arabidopsis thaliana Col-0
-
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 acidsensitivity are even greater in the presence of exogenous S-(2E,6E)-farnesyl-L-cysteine
-
metabolism
-, Q9UHG3
liquid-phase IEF is used to resolve LDL proteins into well-defined fractions on the basis of pI. Besides known LDL-associated proteins, the presence of proteins not previously described to reside in LDL, including prenylcysteine lyase (PCL1) is shown. The finding that an enzyme associated with atherogenic lipoproteins can itself generate an oxidant suggests that PCL1 may play a significant role in atherogenesis
metabolism
-, P57681
the enzyme is involved in the salvage cycle for S-(2E,6E)-farnesyl diphosphate in plants, overview
metabolism
Arabidopsis thaliana Col-0
-
the enzyme is involved in the salvage cycle for S-(2E,6E)-farnesyl diphosphate in plants, overview
-
physiological function
P57681
the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine
physiological function
-, P57681
Arabidopsis FC lyase recognizes amide-linked S-(2E,6E)-farnesyl-L-cysteine and may have a role in deprenylation of farnesylated proteins
physiological function
Arabidopsis thaliana Col-0
-
Arabidopsis FC lyase recognizes amide-linked S-(2E,6E)-farnesyl-L-cysteine and may have a role in deprenylation of farnesylated proteins
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
-, Q9CQF9
-
-
-
?
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
-
-
-
?
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
-
-
-
-
?
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
Q99JK4
-
-
-
?
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
-, Q9UHG3
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
show the reaction diagram
-, Q9CQF9
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
show the reaction diagram
-
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
show the reaction diagram
Q99JK4
-
-
-
?
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
N-acetyl-S-(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
-, P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
N-acetyl-S-(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
Arabidopsis thaliana Col-0
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine, 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
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
S-(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
-, P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
S-(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
Arabidopsis thaliana Col-0
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-, Q9CQF9
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
Q99JK4
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-
kinetic mechanism, enzyme transfers the pro-S hydride of the farnesylcysteine to FAD
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-, Q9CQF9
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
S-(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
-, P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
S-(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
Arabidopsis thaliana Col-0
P57681
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-
kinetic mechanism, enzyme transfers the pro-S hydride of the farnesylcysteine to FAD
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
-, Q9CQF9
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
P57681
required for activity, FC lyase is a flavoprotein
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
diphenyl iodonium
P57681
-
farnesal
-
non-competitive versus farnesyl-L-cysteine
Farnesol
-
non-competitive versus farnesyl-L-cysteine
Farnesol
-, Q9UHG3
dead-end inhibitor
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
P57681
-
-
S-(2E,6E)-farnesyl-L-cysteine
P57681
substrate inhibition
S-(2E,6E)-farnesyl-L-homocysteine
P57681
-
-
geranyl-L-cysteine
P57681
-
-
additional information
P57681
no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
farnesyl-L-cysteine
-
-
0.00069
-
farnesylcysteine
-
-
0.00084
-
geranylgeranylcysteine
-
-
0.05
-
O2
-
Km below
0.045
-
S-(2E,6E)-farnesyl-L-cysteine
P57681
pH 7.5, 30C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000133
-
farnesyl-L-cysteine
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.124
-
diphenyl iodonium
P57681
recombinant enzyme, pH 7.5, 30C
0.194
-
geranyl-L-cysteine
P57681
recombinant enzyme, pH 7.5, 30C
-
0.512
-
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
P57681
recombinant enzyme, pH 7.5, 30C
-
0.05
-
S-(2E,6E)-farnesyl-L-cysteine
P57681
recombinant enzyme, pH 7.5, 30C
0.187
-
S-(2E,6E)-farnesyl-L-homocysteine
P57681
recombinant enzyme, pH 7.5, 30C
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
7.7
-
assay at, depending on type of assay
7.5
-
P57681
assay at
7.5
-
-, P57681
assay at
7.7
-
Q9CQF9
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-, Q9UHG3
assay at
25
-
-
assay at
30
-
P57681
assay at
30
-
-, P57681
assay at
37
-
Q9CQF9
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q9UHG3
VLDL contains a greater protein content of PCL1 than LDL or HDL
Manually annotated by BRENDA team
additional information
-, P57681
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
Manually annotated by BRENDA team
additional information
Arabidopsis thaliana Col-0
-
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55300
-
-, Q9UHG3
mass spectroscopy
63000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P57681
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
P57681
the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene FCLY, encoded on chromosome 5, DNAS and amino acid sequence determination and analysis
-, P57681
gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
P57681
-
Q9CQF9
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
P57681
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
additional information
-, P57681
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
additional information
Arabidopsis thaliana Col-0
-
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
-