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Information on EC 1.8.3.5 - prenylcysteine oxidase and Organism(s) Mus musculus and UniProt Accession Q9CQF9

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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:
Mus musculus
UNIPROT: Q9CQF9
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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: Mus musculus
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
PCLY
-
-
-
-
prenylcysteine lyase
-
-
-
-
prenylcysteine oxidase1
-
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
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
-
-
-
?
S-prenyl-L-cysteine + O2 + H2O
prenal + 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
-
-
-
?
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
physiologic role in cleaving prenylcysteines in mammals, cleaves the thioether bond of prenylcysteines to yield free cysteine and the aldehyde of the isoprenoid lipid
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mouse, wild type and knockout mutants
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PCYOX_MOUSE
505
1
56495
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team