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Literature summary extracted from

  • Frey, P.A.; Reed, G.H.
    Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine (1993), Adv. Enzymol. Relat. Areas Mol. Biol., 66, 1-39.
    View publication on PubMed

Activating Compound

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.3.2 Co2+ enzyme bound cofactor Clostridium sp.
5.4.3.2 Fe2+ Fe-S cluster is required as cofactor Clostridium sp.
5.4.3.2 Fe2+ 12 gatom of iron and of sulfide per mol of hexameric enzyme Clostridium sp.

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.3.2
-
 Clostridium sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.3.2 L-lysine = (3S)-3,6-diaminohexanoate mechanism Clostridium sp.
a
5.4.3.2 L-lysine = (3S)-3,6-diaminohexanoate formation of substrate radicals as intermediates 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
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.2 pyridoxal 5'-phosphate required Clostridium sp.
5.4.3.2 pyridoxal 5'-phosphate contains 5.5 mol of pyridoxal phosphate per mol of hexameric enzyme Clostridium sp.