Literature summary for 3.2.2.9 extracted from

Lee, J.E.; Settembre, E.C.; Cornell, K.A.; Riscoe, M.K.; Sufrin, J.R.; Ealick, S.E.; Howell, P.L.
Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design (2004), Biochemistry, 43, 5159-5169.

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Application

Application	Comment	Organism
medicine	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase is thought to be an ideal target for therapeutic drug design as the enzyme is present in many microbes but not in mammals. The inhibition of MTAN leads to a build-up of toxic byproducts that affect various microbial pathways such as quorum sensing, biological methylation, polyamine biosynthesis, and methionine recycling. The design of nucleosidase-specific inhibitors is complicated by its structural similarity to the human MTA phosphorylase. Structural comparison of 5'-methylthioadenosine phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AF12	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5'-methylthioadenosine + H2O	-	Escherichia coli	5-methylthio-D-ribose + adenine	-	?

Synonyms

Synonyms	Comment	Organism
5'-methylthioadenosine/S-adenosylhomocysteine	-	Escherichia coli
MTA/AdoHcy nucleosidase	-	Escherichia coli
MTAN	-	Escherichia coli

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Release 2023.1 (January 2023)