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Literature summary for 1.8.3.5 extracted from

  • Digits, J.A.; Pyun, H.J.; Coates, R.M.; Casey, P.J.
    Stereospecificity and kinetic mechanism of human prenylcysteine lyase, an unusual thioether oxidase (2002), J. Biol. Chem., 277, 41086-41093.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
farnesal non-competitive versus farnesyl-L-cysteine Homo sapiens
farnesol non-competitive versus farnesyl-L-cysteine Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
farnesyl-L-cysteine
-
Homo sapiens
0.05
-
O2 Km below Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-prenyl-L-cysteine + O2 + H2O Homo sapiens kinetic mechanism, enzyme transfers the pro-S hydride of the farnesylcysteine to FAD prenal + L-cysteine + H2O2
-
?

Organism

Organism UniProt Comment Textmining
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
-
?
S-prenyl-L-cysteine + O2 + H2O
-
Homo sapiens prenal + L-cysteine + H2O2
-
?
S-prenyl-L-cysteine + O2 + H2O kinetic mechanism, enzyme transfers the pro-S hydride of the farnesylcysteine to FAD Homo sapiens prenal + L-cysteine + H2O2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000133
-
farnesyl-L-cysteine
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4 7.7 assay at, depending on type of assay Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens