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Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.5 0.003
-
farnesyl-L-cysteine
-
Homo sapiens
1.8.3.5 0.05
-
O2 Km below Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.5 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

EC Number Organism UniProt Comment Textmining
1.8.3.5 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
-
?
1.8.3.5 S-prenyl-L-cysteine + O2 + H2O
-
Homo sapiens prenal + L-cysteine + H2O2
-
?
1.8.3.5 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.3.5 25
-
assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.3.5 0.000133
-
farnesyl-L-cysteine
-
Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.3.5 7.4 7.7 assay at, depending on type of assay Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.5 FAD
-
Homo sapiens