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Literature summary for 5.4.3.2 extracted from

  • Ballinger, M.D.; Frey, P.A.; Reed, G.H.; LoBrutto, R.
    Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement (1995), Biochemistry, 34, 10086-10093.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

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

Reaction

Reaction Comment Organism Reaction ID
L-lysine = (3S)-3,6-diaminohexanoate evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement, formation of an aldimine linkage between the pyridoxal 5'-phosphate and the beta-nitrogen of (3S)-3,6-diaminohexanoic acid 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 evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement, formation of an aldimine linkage between the pyridoxal 5'-phosphate and the beta-nitrogen of (3S)-3,6-diaminohexanoic acid Clostridium sp.