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Literature summary for 3.5.4.1 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
Search for more literature for 3.5.4.1

Activating Compound

Activating Compound Comment Organism Structure
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

Application Comment Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.19
-
 cytosine pH 7.5, 25°C, wild-type enzyme Escherichia coli
3.9
-
 5-fluorocytosine pH 7.5, 25°C, wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cytosine + H2O Escherichia coli
-
 uracil + NH3
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-fluorocytosine + H2O
-
 Escherichia coli 5-fluorouracil + NH3
-
 ?
cytosine + H2O
-
 Escherichia coli uracil + NH3
-
 ?
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]

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

Turnover Number [1/s]

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

pH Optimum

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