Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in a [4Fe-4S] cluster | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine | Escherichia coli | - |
(3S)-3,6-diaminohexanoate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-lysine = (3S)-3,6-diaminohexanoate | LAM catalytic cycle and reaction intermediate analysis for lysine 2,3-aminomutase | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lysine | - |
Escherichia coli | (3S)-3,6-diaminohexanoate | - |
? | |
additional information | a [4Fe-4S]+ cluster reduces a bound S-adenosylmethionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical. This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes. The strongly oxidizing 5'-deoxyadenosyl radical is quenched by abstracting a H-atom from a target species. Reaction intermediate analysis for lysine 2,3-aminomutase with 4-thia-L-lysine, 13C ENDOR measurements. A close proximity of 5'-dAH to the substrate/product radical is maintained throughout the reaction cycle is thought to minimize the potential for unwanted side reactions of the reactive intermediates and help to recycle S-adenosylmethionine for the next turnover. The pyridoxal 5'-phosphate cofactor plays an important role in stabilizing this species by delocalizing the unpaired electron onto the Pi-system of its pyridine ring yielding N3-(5'-phosphopyridoxylidene)-beta-lysin-2-yl | Escherichia coli | ? | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Escherichia coli | |
S-adenosyl-L-methionine | a [4Fe-4S]+ cluster reduces a bound S-adenosyl-L-methionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical. This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes | Escherichia coli | |
[4Fe-4S] cluster | a [4Fe-4S]+ cluster reduces a bound S-adenosyl-L-methionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical. This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes | Escherichia coli |