The enzyme, originally characterized from the bacterium Rhodospirillum rubrum, is involved in degradation pathways for 5'-deoxyadenosine and S-methyl-5'-thioadenosine, which are formed from S-adenosyl-L-methionine (SAM, AdoMet) by radical SAM enzymes and other types of SAM-dependent enzymes, respectively. The enzyme requires a divalent metal cation, with Co2+ producing the highest activity.
North JA, Wildenthal JA, Erb TJ, Evans BS, Byerly KM, Gerlt JA, Tabita FR
Title
A bifunctional salvage pathway for two distinct S-adenosylmethionine by-products that is widespread in bacteria, including pathogenic Escherichia coli.
