Prenylcysteine oxidase













































prenylcysteine oxidase
Identifiers
EC number 1.8.3.5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile

PDB structures		 RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO















In enzymology, a prenylcysteine oxidase (EC 1.8.3.5) is an enzyme that catalyzes the chemical reaction


an S-prenyl-L-cysteine + O2 + H2O ⇌{displaystyle rightleftharpoons }rightleftharpoons a prenal + L-cysteine + H2O2

The 3 substrates of this enzyme are S-prenyl-L-cysteine, O2, and H2O, whereas its 3 products are prenal, L-cysteine, and H2O2.


This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is S-prenyl-L-cysteine:oxygen oxidoreductase. This enzyme is also called prenylcysteine lyase.



Human protein and gene


  • Prenylcysteine oxidase 1, symbol PCYOX1, gene on chromosome 2


See also




  • Hemithioacetals in nature, for mechanism of action


  • Flavin adenine dinucleotide, cofactor of the enzyme


  • Prenylation, a process forming S-prenyl-L-cysteine



References






  • Zhang L, Tschantz WR, Casey PJ (1997). "Isolation and characterization of a prenylcysteine lyase from bovine brain". J. Biol. Chem. 272 (37): 23354–9. doi:10.1074/jbc.272.37.23354. PMID 9287348..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  • Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ (2001). "Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase". J. Biol. Chem. 276 (4): 2321–4. doi:10.1074/jbc.C000616200. PMID 11078725.








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