Literature summary for 3.5.4.1 extracted from

Hamaji, Y.; Fujimori, M.; Sasaki, T.; Matsuhashi, H.; Matsui-Seki, K.; Shimatani-Shibata, Y.; Kano, Y.; Amano, J.; Taniguchi, S.
Strong enhancement of recombinant cytosine deaminase activity in Bifidobacterium longum for tumor-targeting enzyme/prodrug therapy (2007), Biosci. Biotechnol. Biochem., 71, 874-883.

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Cloned(Commentary)

Cloned (Comment)	Organism
sucloning in strain JM109, construction of a shuttle plasmid Escherichia coli-Bifidobacterium longum, and expression in Bifidobacterium longum strain 105A, expression analysis	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	expression of recombinant cytosine deaminase activity in Bifidobacterium longum results in and strong enhancement of tumor-targeting enzyme/prodrug therapy in human cells, overview	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	-	?

Organism

Organism	UniProt	Comment	Textmining
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	-	?

Temperature Optimum [°C]

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

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Release 2023.1 (January 2023)