Information on EC 1.8.3.5 - prenylcysteine oxidase

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The expected taxonomic range for this enzyme is: Eukaryota

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
1.8.3.5
-
SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
prenylcysteine oxidase
-
SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Terpenoid backbone biosynthesis
-
-
Biosynthesis of antibiotics
-
-
SplaateSystematic_Name,Commentary_IUBMB
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.
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
EC 4.4.1.18
-
-
formerly
-
farnesylcysteine lyase
-
FC lyase
Arabidopsis thaliana Col-0
-
-
FCLY
Arabidopsis thaliana Col-0
gene name
-
flavin adenine dinucleotide (FAD)-dependent thioether oxidase
-
-
PCL
-
-
PCLY
-
-
-
-
prenylcysteine lyase
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-
-
-
prenylcysteine lyase
-
-
prenylcysteine lyase
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prenylcysteine oxidase1
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SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
196717-99-4
-
SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
SplaateGeneral_Information, Organism, Commentary, Literature
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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 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
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
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
the specific farnesylcysteine lyase is responsible for the oxidative metabolism of FC to farnesal and cysteine
physiological function
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
-
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
-
-
?
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
-
-
?
farnesyl-L-cysteine + O2 + H2O
farnesal + L-cysteine + H2O2
show the reaction diagram
-
-
?
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
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
show the reaction diagram
-
-
?
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Col-0
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
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
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
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
(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
Arabidopsis thaliana Col-0
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
-
-
?
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
-
-
?
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
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
-
?
SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
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
(2E,6E)-farnesal + L-cysteine + H2O2
show the reaction diagram
Arabidopsis thaliana, 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
-
?
SplaateCofactor,Organism,Commentary,Literature,Filename
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
required for activity, FC lyase is a flavoprotein
SplaateMetals_Ions,Organism,Commentary, Literature
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphenyl iodonium
-
farnesal
-
non-competitive versus farnesyl-L-cysteine
Farnesol
-
non-competitive versus farnesyl-L-cysteine
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
-
S-(2E,6E)-farnesyl-L-cysteine
substrate inhibition
S-(2E,6E)-farnesyl-L-homocysteine
-
S-geranyl-L-cysteine
-
Farnesol
dead-end inhibitor
additional information
no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine
-
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
-
SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
pH 7.5, 30C
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000133
farnesyl-L-cysteine
Homo sapiens
-
-
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.124
diphenyl iodonium
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.512
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.05
S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.187
S-(2E,6E)-farnesyl-L-homocysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
0.194
S-geranyl-L-cysteine
Arabidopsis thaliana
P57681
recombinant enzyme, pH 7.5, 30C
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 7.7
-
assay at, depending on type of assay
7.7
assay at
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
assay at
25
-
assay at
37
assay at
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
VLDL contains a greater protein content of PCL1 than LDL or HDL
Manually annotated by BRENDA team
additional information
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
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Arabidopsis thaliana Col-0
-
-
-
Manually annotated by BRENDA team
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55300
mass spectroscopy
706670
63000
-
SDS-PAGE
669763
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
SplaatePosttranslational_Modification, Organism, Commentary, Literature
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
SplaateCommentary, Organism, Literature
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
SplaateGeneral_Stability, Organism, Literature
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
column chromatography
-
SplaateCommentary, Organism, Literature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene FCLY, encoded on chromosome 5, DNAS and amino acid sequence determination and analysis
gene FCLY, functional expression in Spodoptera frugiperda Sf9 cells using the recombinant baculovirus transfection system.
SplaateCommentary, Organism, Literature
SplaateEngineering, Organism, Commentary, Literature
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
-
SplaateCommentary, Organism, Literature
SplaateApplication,Organism,Commentary,Literature