Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.3.2 extracted from

  • Stich, T.A.; Myers, W.K.; Britt, R.D.
    Paramagnetic intermediates generated by radical S-adenosylmethionine (SAM) enzymes (2014), Acc. Chem. Res., 47, 2235-2243 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.3.2

Inhibitors

Inhibitors Comment Organism Structure
Fe2+ in a [4Fe-4S] cluster Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Escherichia coli
-
 (3S)-3,6-diaminohexanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

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
a

Substrates and Products (Substrate)

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

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