EC Number   |
Cofactor |
Reference |
|---|
   4.1.99.14 | S-adenosyl-L-methionine |
- |
677516, 680717, 714747, 715668 |
| 4.1.99.14 | S-adenosyl-L-methionine |
a radical S-adenosyl-L-methionine enzyme that uses a [4Fe-4S]1+ cluster and S-adenosyl-L-methionine to initiate the repair reaction |
728401 |
| 4.1.99.14 | S-adenosyl-L-methionine |
a radical S-adenosyl-L-methionine enzyme that uses a [4Fe-4S]1+ cluster to reduce the S-adenosyl-L-methionine generating a catalytic 5'-deoxyadenosyl radical |
726998, 727020 |
| 4.1.99.14 | S-adenosyl-L-methionine |
a radical S-adenosyl-L-methionine enzyme, S-adenosyl-L-methionine is suggested to be regenerated at the end of each catalytic cycle, and only a catalytic amount of S-adenosyl-L-methionine is needed in the enzyme reaction. The H atom source for the back donation step is suggested to be a cysteine residue 141, and the H-atom transfer reaction leaves a thiyl radical behind on the protein. This thiyl radical thus must participate in the S-adenosyl-L-methionine regeneration process, the thiyl radical abstracts an H atom from the 5'-deoxyadenosyl radical to regenerate S-adenosyl-L-methionine |
727074 |
| 4.1.99.14 | S-adenosyl-L-methionine |
a radical SAM enzyme |
727295 |
| 4.1.99.14 | S-adenosyl-L-methionine |
SAM, SPL is a radical SAM enzyme and requires S-adenosyl-L-methionine (SAM) for catalysis. Density functional theory calculations provide insights into structural and electronic perturbations that can be correlated by considering the role of SAM as a catalyst or substrate. Mapping of the [4Fe-4S]/SAM interaction, and speciation dependent SAM/cluster interactions |
748241 |
| 4.1.99.14 | S-adenosyl-L-methionine |
SAM, SPL is a radical SAM enzyme, enzyme SPL has low affinity for substrate or DNA in the absence of SAM. SAM causes significant structural perturbations regardless of the integrity of the iron-sulfur cluster, consistent with the observation that SAM binds SPL not only via coordination of the iron-sulfur cluster, but also by interactions such as hydrogen bonding, hydrophobic interactions and salt bridges. The amino group of the methionyl moiety of SAM interacts with Ser142 and Asp143 and the carboxylate moiety interacts with Lys174 and Ser195, while the adenine and ribose groups are held in place via hydrogen bonding interactions with Tyr96, Tyr98, Ala234 and Ala273 |
747765 |
| 4.1.99.14 | S-adenosyl-L-methionine |
SPL is a radical SAM enzyme |
747506, 747639, 747837, 748201, 748849, 748852 |
| 4.1.99.14 | S-adenosyl-L-methionine |
the enzyme is an S-adenosylmethionine-dependent iron-sulfur protein that belongs to the radical S-adenosylmethionine superfamily |
680685 |
| 4.1.99.14 | [4Fe-4S] cluster |
- |
747506, 747765 |
