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Literature summary for 5.4.3.2 extracted from

  • Wang, S.C.; Frey, P.A.
    Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme (2007), Biochemistry, 46, 12889-12895.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.3.2

Cloned(Commentary)

Cloned (Comment) Organism
-
 Clostridium subterminale

Metals/Ions

Metals/Ions Comment Organism Structure
Iron [4Fe-4S] cluster. Reduction potential for the cluster is lowered by 0.17 V by the binding of lysine to enzyme, and the binding of S-adenosyl-L-methionine to the cluster elevates its reduction potential by 0.81 V. Thus binding of L-lysine and S-adenosylmethionine lower the barrier for reductive cleavage of S-adenosylmethionine at the active site from 32 kcal per mol to 9 kcal per mol Clostridium subterminale

Organism

Organism UniProt Comment Textmining
Clostridium subterminale
-
-
-
Clostridium subterminale SB4
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium subterminale

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
 Clostridium subterminale (3S)-3,6-diaminohexanoic acid
-
 ?
L-lysine
-
 Clostridium subterminale SB4 (3S)-3,6-diaminohexanoic acid
-
 ?

Synonyms

Synonyms Comment Organism
LAM
-
 Clostridium subterminale
lysine 2,3-aminomutase
-
 Clostridium subterminale

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center
-
 Clostridium subterminale