Literature summary for 3.2.2.9 extracted from

Xu, Y.; Wang, L.; Chen, J.; Zhao, J.; Fan, S.; Dong, Y.; Ha, N.C.; Quan, C.
Structural and functional analyses of periplasmic 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Aeromonas hydrophila (2017), Biochemistry, 56, 5347-5355 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of MtaN-1 in its apo form and in complex with substrates S-adenosyl-L-homocysteine, 5'-methylthioadenosine, and 5'-deoxyadenosine. MtaN-1 has an extension of the binding pocket and a tryptophan in the active site (Trp199) may play a major role in substrate binding	Aeromonas hydrophila subsp. hydrophila

Protein Variants

Protein Variants	Comment	Organism
W199A	mutation completely abolishes the enzyme activity	Aeromonas hydrophila subsp. hydrophila

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Aeromonas hydrophila subsp. hydrophila	-	-

Organism

Organism	UniProt	Comment	Textmining
Aeromonas hydrophila subsp. hydrophila	A0KGU9	-	-
Aeromonas hydrophila subsp. hydrophila DSM 30187	A0KGU9	-	-

Synonyms

Synonyms	Comment	Organism
Mtan-1	-	Aeromonas hydrophila subsp. hydrophila

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Release 2023.1 (January 2023)