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Literature summary extracted from

  • Li, C.; Wildes, F.; Winnard, P.; Artemov, D.; Penet, M.F.; Bhujwalla, Z.M.
    Conjugation of poly-L-lysine to bacterial cytosine deaminase improves the efficacy of enzyme/prodrug cancer therapy (2008), J. Med. Chem., 51, 3572-3582.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.4.1 additional information conjugation of poly-L-lysine to cytosine deaminase improves the efficacy of enzyme/prodrug cancer therapy, e.g. by a 50times higher cellular uptake than that of control molecules in human breast MDA-MB-231 cancer cells and increase stability after uptake into cells, uptake and intracellular distribution, mechanisms, overview Escherichia coli

Application

EC Number Application Comment Organism
3.5.4.1 medicine the enzyme is useful in gene therapy of cancers, conjugation of poly-L-lysine to cytosine deaminase improves the efficacy of enzyme/prodrug cancer therapy, overview Escherichia coli

General Stability

EC Number General Stability Organism
3.5.4.1 conjugation of poly-L-lysine to cytosine deaminase increases the enzyme's stability after uptake into cells, mechanism, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.1 additional information
-
 additional information the kinetics of the enzyme associated with poly-L-lysine derivatives are very similar to the wild-type enzyme kinetics, overview Escherichia coli
3.5.4.1 0.19
-
 cytosine pH 7.5, 25°C, wild-type enzyme Escherichia coli
3.5.4.1 3.9
-
 5-fluorocytosine pH 7.5, 25°C, wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.1 cytosine + H2O Escherichia coli
-
 uracil + NH3
-
 ?
3.5.4.1 additional information Escherichia coli the enzyme is useful in gene therapy of cancers, conjugation of poly-L-lysine to cytosine deaminase improves the efficacy of enzyme/prodrug cancer therapy, e.g. by a 50times higher cellular uptake than that of control molecules in human breast MDA-MB-231 cancer cells and increase stability after uptake into cells, uptake and intracellular distribution, mechanisms, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.1 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.4.1 58
-
 wild-type enzyme, substrate 5-fluorocytosine Escherichia coli
3.5.4.1 144
-
 wild-type enzyme, substrate cytosine Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.1 5-fluorocytosine + H2O
-
 Escherichia coli 5-fluorouracil + NH3
-
 ?
3.5.4.1 cytosine + H2O
-
 Escherichia coli uracil + NH3
-
 ?
3.5.4.1 additional information the enzyme is useful in gene therapy of cancers, conjugation of poly-L-lysine to cytosine deaminase improves the efficacy of enzyme/prodrug cancer therapy, e.g. by a 50times higher cellular uptake than that of control molecules in human breast MDA-MB-231 cancer cells and increase stability after uptake into cells, uptake and intracellular distribution, mechanisms, overview Escherichia coli ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.1 25
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.4.1 71
-
 5-fluorocytosine pH 7.5, 25°C, wild-type enzyme Escherichia coli
3.5.4.1 185
-
 cytosine pH 7.5, 25°C, wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.1 7.5
-
 assay at Escherichia coli