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Literature summary extracted from

  • 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 (2009), Proteomics, 9, 1344-1352.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.3.5 farnesol dead-end inhibitor Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.3.5 55300
-
mass spectroscopy Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.5 Homo sapiens Q9UHG3
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.5 blood plasma VLDL contains a greater protein content of PCL1 than LDL or HDL Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.5 farnesyl-L-cysteine + O2 + H2O
-
Homo sapiens farnesal + L-cysteine + H2O2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.3.5 PCL1
-
Homo sapiens
1.8.3.5 prenylcysteine lyase
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.3.5 23
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.5 FAD
-
Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.3.5 metabolism 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 Homo sapiens