1.8.3.5: prenylcysteine oxidase
This is an abbreviated version!
For detailed information about prenylcysteine oxidase, go to the full flat file.
Word Map on EC 1.8.3.5
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1.8.3.5
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polycaprolactone
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posterior
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ligament
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cruciate
-
knee
-
fabric
-
electrospun
-
fiber
-
biocompatibility
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electrospinning
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tibial
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nanofibers
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porous
-
copolymer
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blend
-
film
-
flexion
-
modulus
-
tensile
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biomaterials
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femoral
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nanofibrous
-
arthroscopic
-
porosity
-
biomechanical
-
polyepsilon-caprolactone
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tendon
-
tear
-
laxity
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arthroplasty
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kinematics
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posterolateral
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avulsion
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posteromedial
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lysholm
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polyester
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autograft
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bioresorbable
-
hamstring
-
osteoconductive
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meniscal
-
wettabl
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varus
-
diblock
-
cytocompatibility
-
condyle
-
anterolateral
-
polylactic
-
wettability
-
tissue-engineered
- 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
Reaction
Synonyms
EC 4.4.1.18, farnesylcysteine lyase, FC lyase, FCLY, flavin adenine dinucleotide (FAD)-dependent thioether oxidase, PCL, PCL1, PCLY, PCYOX, PCYOX1, prenylcysteine lyase, prenylcysteine oxidase 1, prenylcysteine oxidase1
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Reference
Reference on EC 1.8.3.5 - prenylcysteine oxidase
Please use the Reference Search for a specific query.
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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
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
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
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
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
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)
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)
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
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