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Literature summary extracted from

  • Baraniak, J.; Moss, M.L.; Frey, P.A.
    Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine (1989), J. Biol. Chem., 264, 1357-1360.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.3.2 S-adenosylmethionine activates Clostridium sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.3.2 Fe2+ contains iron Clostridium sp.

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.2 Clostridium sp.
-
-
-
5.4.3.2 Clostridium sp. SB4
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.3.2 L-lysine = (3S)-3,6-diaminohexanoate activation of the enzyme may involve a transformation of S-adenosylmethionine into a form that promotes the generation of an adenosyl-5' free radical, which abstracts hydrogen from Lys to form 5'-deoxyadenosine as an intermediate Clostridium sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.2 L-Lys
-
 Clostridium sp. (3S)-3,6-diaminohexanoic acid
-
 ?
5.4.3.2 L-Lys
-
 Clostridium sp. SB4 (3S)-3,6-diaminohexanoic acid
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.2 pyridoxal 5'-phosphate contains pyridoxal phosphate Clostridium sp.