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Literature summary for 5.4.3.2 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
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Activating Compound

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-
Clostridium sp. SB4
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Cofactor

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