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Information on EC 1.8.3.5 - prenylcysteine oxidase and Organism(s) Homo sapiens and UniProt Accession Q9UHG3

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EC Tree
     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.3 With oxygen as acceptor
                1.8.3.5 prenylcysteine oxidase
IUBMB 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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This record set is specific for:
Homo sapiens
UNIPROT: Q9UHG3
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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 taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
pcl, prenylcysteine lyase, pcyox1, fc lyase, prenylcysteine oxidase 1, prenylcysteine oxidase1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
prenylcysteine lyase
-
prenylcysteine oxidase 1
-
PCLY
-
-
-
-
prenylcysteine lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
196717-99-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an S-prenyl-L-cysteine + O2 + H2O
a prenal + 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
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + L-cysteine + H2O2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
farnesol
dead-end inhibitor
farnesal
-
non-competitive versus farnesyl-L-cysteine
farnesol
-
non-competitive versus farnesyl-L-cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
farnesyl-L-cysteine
-
-
0.05
O2
-
Km below
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000133
farnesyl-L-cysteine
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.7
-
assay at, depending on type of assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
assay at
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
VLDL contains a greater protein content of PCL1 than LDL or HDL
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PCYOX_HUMAN
505
0
56640
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55300
mass spectroscopy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team