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Literature summary for 5.4.3.2 extracted from

  • Chen, D.; Walsby, C.; Hoffman, B.M.; Frey, P.A.
    Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase (2003), J. Am. Chem. Soc., 125, 11788-11789.
    View publication on PubMed
Search for more literature for 5.4.3.2

Metals/Ions

Metals/Ions Comment Organism Structure
Iron LAM contains an [4Fe-4S]+ cluster Clostridium subterminale

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Clostridium subterminale initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia (3S)-3,6-diaminohexanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium subterminale
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia Clostridium subterminale (3S)-3,6-diaminohexanoate
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 ?

Synonyms

Synonyms Comment Organism
LAM
-
 Clostridium subterminale

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Clostridium subterminale
S-adenosyl-L-methionine
-
 Clostridium subterminale