EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.5.1.B21 | 5'-deoxy-5'-chloroadenosine + H2O |
adenosine is generated from 5'-deoxy-5'-chloroadenosine with much lower efficiency than from S-adenosyl-L-methionine |
Pyrococcus horikoshii |
adenosine + ? |
- |
? |
2.5.1.B21 | 5'-deoxy-5'-chloroadenosine + H2O |
adenosine is generated from 5'-deoxy-5'-chloroadenosine with much lower efficiency than from S-adenosyl-L-methionine |
Pyrococcus horikoshii OT-3 |
adenosine + ? |
- |
? |
2.5.1.B21 | S-adenosyl-L-methionine + H2O |
- |
Salinispora arenicola |
adenosine + L-methionine + H+ |
- |
? |
2.5.1.B21 | S-adenosyl-L-methionine + H2O |
the enzyme is most active at pH 8.5, so perhaps it has a regulatory role in influencing the cellular pH in the host organism. Many, but not all of the duf-62 containing organisms are extremophiles |
Pyrococcus horikoshii |
adenosine + L-methionine + H+ |
- |
? |
2.5.1.B21 | S-adenosyl-L-methionine + H2O |
conversion of S-adenosyl-L-methionine into adenosine by the attack of a hydroxide ion from water at C5 of S-adenosyl-L-methionine. No new products are detected by HPLC or NMR spectroscopy after the incubation of the enzyme with S-adenosyl-L-methionine and F-, Cl-, or NH4+ ions at high mM concentrations. In all cases adenosine is generated in a manner consistent with normal enzymatic turnover, with water providing the nucleophil |
Pyrococcus horikoshii |
adenosine + L-methionine + H+ |
- |
? |
2.5.1.B21 | S-adenosyl-L-methionine + H2O |
mechanistic hypothesis for SAM hydroxide adenosyltransferase |
Pyrococcus horikoshii |
adenosine + L-methionine + H+ |
- |
? |
2.5.1.B21 | S-adenosyl-L-methionine + H2O |
the amino acid Asp-Arg-His triad and particularly the Asp-Arg ion pair appears to play an important role in holding the water for nucleophilic attack as S-adenosyl-L-methionine binds and becomes proximate |
Pyrococcus horikoshii |
adenosine + L-methionine + H+ |
- |
? |
2.5.1.B21 | S-adenosyl-L-methionine + H2O |
conversion of S-adenosyl-L-methionine into adenosine by the attack of a hydroxide ion from water at C5 of S-adenosyl-L-methionine. No new products are detected by HPLC or NMR spectroscopy after the incubation of the enzyme with S-adenosyl-L-methionine and F-, Cl-, or NH4+ ions at high mM concentrations. In all cases adenosine is generated in a manner consistent with normal enzymatic turnover, with water providing the nucleophil |
Pyrococcus horikoshii OT-3 |
adenosine + L-methionine + H+ |
- |
? |