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Literature summary extracted from

  • Zappia, V.; Barker, H.A.
    Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups (1970), Biochim. Biophys. Acta, 207, 505-513.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.3.2 iodoacetic acid
-
 Clostridium sp.
5.4.3.2 NEM
-
 Clostridium sp.
5.4.3.2 PCMB
-
 Clostridium sp.
5.4.3.2 SDS 50 mM, the rate of inactivation decreases in the presence of L-Lys, S-adenosylmethionine or S-adenosylhomocysteine. The SDS-dissociated enzyme can be slightly reactivated by removal of the detergent by gel filtration or dialysis Clostridium sp.
5.4.3.2 Urea 4 M Clostridium sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.3.2 48000
-
 6 * 48000, SDS-PAGE Clostridium sp.

Organism

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

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
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.3.2 hexamer 6 * 48000, SDS-PAGE Clostridium sp.