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Information on EC 1.8.3.5 - prenylcysteine oxidase
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EC Tree
1.8.3.5 prenylcysteine oxidaseIUBMB Comments
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.
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Word Map
- 1.8.3.5
-
polycaprolactone
-
posterior
-
ligament
-
cruciate
- knee
-
fabric
-
electrospun
- fiber
-
biocompatibility
-
electrospinning
- tibial
-
nanofibers
-
porous
- copolymer
-
blend
-
film
-
flexion
-
modulus
-
tensile
-
biomaterials
- femoral
-
nanofibrous
-
arthroscopic
-
porosity
-
biomechanical
-
polyepsilon-caprolactone
- tendon
- tear
- laxity
-
arthroplasty
-
kinematics
-
posterolateral
-
avulsion
-
posteromedial
-
lysholm
-
polyester
-
autograft
-
bioresorbable
-
hamstring
-
osteoconductive
- meniscal
-
wettabl
- varus
-
diblock
-
cytocompatibility
-
condyle
-
anterolateral
-
polylactic
-
wettability
-
tissue-engineered
The enzyme appears in viruses and cellular organisms
Synonyms
pcl, prenylcysteine lyase, pcyox1, fc lyase, prenylcysteine oxidase 1, prenylcysteine oxidase1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 4.4.1.18
-
-
formerly
-
FC lyase
FCLY
PCLY
-
-
-
-
prenylcysteine lyase
prenylcysteine lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
-
-
-
-
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
kinetics and catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
196717-99-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
-
-
-
?
geranylgeranyl-L-cysteine + O2 + H2O
geranylgeranal + L-cysteine + H2O2
-
-
-
?
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + N-acetyl-L-cysteine + H2O2
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
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
-
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
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
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
-
kinetic mechanism, enzyme transfers the pro-S hydride of the farnesylcysteine to FAD
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-(2E,6E)-farnesyl-L-cysteine + O2 + H2O
(2E,6E)-farnesal + L-cysteine + H2O2
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
-
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
the enzyme exhibits specificity for farnesyl-L-cysteine over geranylgeranyl-L-cysteine
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
-
kinetic mechanism, enzyme transfers the pro-S hydride of the farnesylcysteine to FAD
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by geranylgeranyl-L-cysteine, benzylcysteine, citronellylcysteine, and nerylcysteine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.512
N-acetyl-S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
recombinant enzyme, pH 7.5, 30°C
0.05
S-(2E,6E)-farnesyl-L-cysteine
Arabidopsis thaliana
recombinant enzyme, pH 7.5, 30°C
0.187
S-(2E,6E)-farnesyl-L-homocysteine
Arabidopsis thaliana
recombinant enzyme, pH 7.5, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
VLDL contains a greater protein content of PCL1 than LDL or HDL
brenda
additional information
additional information
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
brenda
additional information
-
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
brenda
additional information
-
the enzyme is ubiquitously expressed in Arabidopsis tissues and organs
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
-
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
apart from transporting lipids through the body, the human plasma lipoproteins very low-density lipoprotein (VLDL) and low-density lipoprotein (LDL) are also thought to serve as a modality for intra-organismal protein transfer, shipping proteins with important roles in inflammation and thrombosis from the site of synthesis to effector locations. Prenylcysteine oxidase 1, like dermcidin, cathelicidin antimicrobial peptide, TFPI-1 and fibrinogen alpha chain, is associated with both VLDL and LDL in human plasma. Analysis of VLDL- and LDL-associated proteins, overview
metabolism
-
the enzyme is involved in the salvage cycle for S-(2E,6E)-farnesyl diphosphate in plants, overview
-
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
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PCYOX_BOVIN
508
0
56776
Swiss-Prot
Secretory Pathway (Reliability: 2)
PCYOX_HUMAN
505
0
56640
Swiss-Prot
Secretory Pathway (Reliability: 1)
PCYOX_MACFA
505
0
56517
Swiss-Prot
Secretory Pathway (Reliability: 1)
PCYOX_MOUSE
505
1
56495
Swiss-Prot
Secretory Pathway (Reliability: 1)
PCYOX_PONAB
505
0
56752
Swiss-Prot
Secretory Pathway (Reliability: 1)
PCYOX_RAT
504
0
56288
Swiss-Prot
Secretory Pathway (Reliability: 2)
B9PW39_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
611
0
68137
TrEMBL
Secretory Pathway (Reliability: 2)
A0A086JKE4_TOXGO
611
0
68106
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2I0BB95_9ASPA
499
0
55916
TrEMBL
Secretory Pathway (Reliability: 1)
S8ETF6_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
611
0
68062
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7R8H7A1_LEPSM
410
0
46153
TrEMBL
other Location (Reliability: 3)
B7ZTK4_XENTR
501
0
55766
TrEMBL
Secretory Pathway (Reliability: 1)
K0KUT7_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
480
0
53908
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3R8BTR4_TOXGO
611
0
68106
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3M7QB50_BRAPC
511
1
58760
TrEMBL
other Location (Reliability: 3)
M5BQ22_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
422
0
45594
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9HKC0_9LAMI
493
0
54783
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2I0ATQ6_9ASPA
369
1
41715
TrEMBL
other Location (Reliability: 3)
A0A125YHU5_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
611
0
68137
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3M7SA64_BRAPC
634
0
73735
TrEMBL
other Location (Reliability: 1)
A0A3G2S550_9BASI
554
0
61369
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8B6ET55_MYTGA
489
0
54769
TrEMBL
Secretory Pathway (Reliability: 3)
A0A6J8B3Q9_MYTCO
490
0
54881
TrEMBL
Secretory Pathway (Reliability: 1)
E0VQZ6_PEDHC
495
0
56286
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G8XWP6_TOXGO
611
0
68123
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2T6IHM1_TOXGO
611
0
68106
TrEMBL
Secretory Pathway (Reliability: 2)
A0A086PUD5_TOXGO
611
0
68123
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5B7BD05_DAVIN
489
0
54336
TrEMBL
Chloroplast (Reliability: 5)
A0A812CFS5_SEPPH
397
0
45406
TrEMBL
other Location (Reliability: 2)
A0A1Z5JLW9_FISSO
567
0
61752
TrEMBL
Secretory Pathway (Reliability: 1)
A0A086M0M3_TOXGO
611
0
68137
TrEMBL
Secretory Pathway (Reliability: 2)
A0A086JHK2_TOXGO
611
0
68062
TrEMBL
Secretory Pathway (Reliability: 3)
A0A139XWE0_TOXGO
611
0
68062
TrEMBL
Secretory Pathway (Reliability: 3)
A0A086Q4A6_TOXGO
611
0
68125
TrEMBL
Secretory Pathway (Reliability: 2)
A0A364NAG6_9PLEO
837
0
92448
TrEMBL
other Location (Reliability: 5)
A0A086JXY2_TOXGO
611
0
68171
TrEMBL
Secretory Pathway (Reliability: 2)
Q568K1_DANRE
509
0
56672
TrEMBL
Secretory Pathway (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
55300
67000
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
55300
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 67000, recombinant enzyme, SDS-PAGE, x * 55300, about, sequence calculation, x * 55000, deglycosylated recombinant enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the FCLY gene possesses a predicted amino terminal signal sequence and four putative N-glycosylation sites
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beigneux, A.; Withycombe, S.K.; Digits, J.A.; Tschantz, W.R.; Weinbaum, C.A.; Griffey, S.M.; Bergo, M.; Casey, P.J.; Young, S.G.
Prenylcysteine lyase deficiency in mice results in the accumulation of farnesylcysteine and geranylgeranylcysteine in brain and liver
J. Biol. Chem.
277
38358-38363
2002
Mus musculus (Q9CQF9), Mus musculus
brenda
Digits, J.A.; Pyun, H.J.; Coates, R.M.; Casey, P.J.
Stereospecificity and kinetic mechanism of human prenylcysteine lyase, an unusual thioether oxidase
J. Biol. Chem.
277
41086-41093
2002
Homo sapiens
brenda
Wouters, M.M.; Neefs, J.M.; Kerchove dExaerde, A.; Vanderwinden, J.M.; Smans, K.A.
Downregulation of two novel genes in Sl/Sld and W(LacZ)/Wv mouse jejunum
Biochem. Biophys. Res. Commun.
346
491-500
2006
Mus musculus (Q99JK4), Mus musculus
brenda
Lu, J.Y.; Hofmann, S.L.
Thematic review series: lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins
J. Lipid Res.
47
1352-1357
2006
Bos taurus
brenda
Banfi, C.; Brioschi, M.; Barcella, S.; Wait, R.; Begum, S.; Galli, S.; Rizzi, A.; Tremoli, E.
Proteomic analysis of human low-density lipoprotein reveals the presence of prenylcysteine lyase, a hydrogen peroxide-generating enzyme
Proteomics
9
1344-1352
2009
Homo sapiens (Q9UHG3), Homo sapiens
brenda
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
Mol. Plant
3
143-155
2010
Arabidopsis thaliana (P57681)
brenda
Crowell, D.N.; Huizinga, D.H.; Deem, A.K.; Trobaugh, C.; Denton, R.; Sen, S.E.
Arabidopsis thaliana plants possess a specific farnesylcysteine lyase that is involved in detoxification and recycling of farnesylcysteine
Plant J.
50
839-847
2007
Arabidopsis thaliana (P57681), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (P57681)
brenda
Dashty, M.; Motazacker, M.M.; Levels, J.; de Vries, M.; Mahmoudi, M.; Peppelenbosch, M.P.; Rezaee, F.
Proteome of human plasma very low-density lipoprotein and low-density lipoprotein exhibits a link with coagulation and lipid metabolism
Thromb. Haemost.
111
518-530
2014
Homo sapiens (Q9UHG3), Homo sapiens