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Literature summary for 1.8.3.5 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

Inhibitors Comment Organism Structure
farnesol dead-end inhibitor Homo sapiens

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UHG3
-
-

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PCL1
-
Homo sapiens
prenylcysteine lyase
-
Homo sapiens

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens

General Information

General Information Comment Organism
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