Literature summary for 3.2.2.9 extracted from

Dorgan, K.M.; Wooderchak, W.L.; Wynn, D.P.; Karschner, E.L.; Alfaro, J.F.; Cui, Y.; Zhou, Z.S.; Hevel, J.M.
An enzyme-coupled continuous spectrophotometric assay for S-adenosylmethionine-dependent methyltransferases (2006), Anal. Biochem., 350, 249-255.

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Application

Application	Comment	Organism
analysis	enzyme-coupled continuous spectrophotometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)-dependent methyltransferase activity. In this assay, S-adenosyl-L-homocysteine, the transmethylation product of AdoMet-dependent methyltransferases, is hydrolyzed to S-ribosylhomocysteine and adenine by recombinant S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Subsequently, adenine generated from AdoHcy is further hydrolyzed to hypoxanthine and ammonia by recombinant adenine deaminase. Application of the assay to other enzymes that produce S-adenosylhomocysteine	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
expression with His-tag	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	enzyme-coupled continuous spectrophotometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)-dependent methyltransferase activity. In this assay, S-adenosyl-L-homocysteine, the transmethylation product of AdoMet-dependent methyltransferases, is hydrolyzed to S-ribosylhomocysteine and adenine by recombinant S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Subsequently, adenine generated from AdoHcy is further hydrolyzed to hypoxanthine and ammonia by recombinant adenine deaminase	Escherichia coli

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Release 2023.1 (January 2023)