EC Number   |
Reaction |
Reference |
|---|
    3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
- |
- |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
early dissociative transition state |
677284 |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
early SN1 transition state with significant N-glycosidic bond order at the transition state |
680360 |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
late dissociative transition state |
677284 |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
mechanism |
656196 |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
SN1 transition state with no covalent participation of the adenine or the water nucleophile. Isotope effects predict a 3-endo conformation for the ribosyl oxacarbenium-ion transition state. The N7 of the leaving group adenine is not protonated in the transition state |
680367 |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
structure-function analysis and reaction mechanism, overview. The proposed mechanism of action for the hydrolysis of methylthioadenosine by the enzyme involves the essential acidic residue in the lid of the active site and a water molecule that acts as a nucleophile which is activated by an arginine and a glutamic acid residue |
726595 |
| 3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine |
transitions state analogues, overview |
731300 |
