Literature summary for 2.4.2.4 extracted from

Petaccia, M.; Gentili, P.; Besker, N.; DAbramo, M.; Giansanti, L.; Leonelli, F.; La Bella, A.; Gradella Villalva, D.; Mancini, G.
Kinetics and mechanistic study of competitive inhibition of thymidine phosphorylase by 5-fluoruracil derivatives (2016), Colloids Surf. B Biointerfaces, 140, 121-127.

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Inhibitors

Inhibitors	Comment	Organism	Structure
5-fluoro-1-(3,6,9,12,15,18,21,24-octaoxahexatriacontan-1-yl)pyrimidine-2,4(1H,3H)-dione	43% competitive inhibition at 0.04 mM	Escherichia coli
5-fluoro-1-(3,6,9,12,15,18,21-heptaoxatritriacontan-1-yl)pyrimidine-2,4(1H,3H)-dione	40% competitive inhibition at 0.04 mM	Escherichia coli
5-fluoro-1-(3,6,9,12,15,18-hexaoxatriacontan-1-yl)pyrimidine-2,4(1H,3H)-dione	38% competitive inhibition at 0.04 mM	Escherichia coli
5-fluorouracil	38% inhibition at 0.04 mM	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.19	-	thymidine	at pH 7.4 and 37°C	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
thymidine + phosphate	Escherichia coli	-	thymine + 2-deoxy-alpha-D-ribose 1-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P07650	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
thymidine + phosphate	-	Escherichia coli	thymine + 2-deoxy-alpha-D-ribose 1-phosphate	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
130	-	thymidine	at pH 7.4 and 37°C	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0042	-	5-fluorouracil	at pH 7.4 and 37°C	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
680	-	thymidine	at pH 7.4 and 37°C	Escherichia coli

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Release 2023.1 (January 2023)