Literature summary extracted from

Shugart, L.; Mahoney, L.; Chastain, B.
Kinetic studies of Drosophila melanogaster methylthioadenosine nucleoside phosphorylase (1981), Int. J. Biochem., 13, 559-564.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.4.2.28	0.0055	-	5'-methylthioadenosine	-	Drosophila melanogaster
2.4.2.28	13.5	-	phosphate	-	Drosophila melanogaster

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.2.28	Drosophila melanogaster	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.4.2.28	S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate	ordered bisubstrate biproduct reaction with methylthioadenosine the first substrate to add and adenine the last product to leave the enzyme	Drosophila melanogaster	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.4.2.28	5'-methylthioadenosine + phosphate	-	Drosophila melanogaster	adenine + 5-methylthio-D-ribose 1-phosphate	-	?

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Release 2023.1 (January 2023)