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
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knee
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fabric
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electrospun
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fiber
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biocompatibility
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electrospinning
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tibial
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nanofibers
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porous
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copolymer
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blend
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film
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flexion
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modulus
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tensile
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biomaterials
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femoral
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nanofibrous
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arthroscopic
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porosity
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biomechanical
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polyepsilon-caprolactone
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tendon
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tear
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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
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hamstring
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osteoconductive
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meniscal
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wettabl
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varus
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diblock
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cytocompatibility
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condyle
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anterolateral
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polylactic
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wettability
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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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General Information
General Information on EC 1.8.3.5 - prenylcysteine oxidase
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malfunction
metabolism
physiological function
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
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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
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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
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the enzyme is involved in the salvage cycle for S-(2E,6E)-farnesyl diphosphate in plants, overview
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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
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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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