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Literature summary extracted from

  • Petrovich, R.M.; Ruzicka, F.J.; Reed, G.H.; Frey, P.A.
    Metal cofactors of lysine-2,3-aminomutase (1991), J. Biol. Chem., 266, 7656-7660.
    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+ contains 3.5 gatom of cobalt per mol of enzyme Clostridium sp.
5.4.3.2 Co2+ enzyme bound cofactor Clostridium sp.
5.4.3.2 Cu2+ enzyme-bound, occupies cobalt sites in the enzyme under conditions of insufficient cobalt in the growth medium, even the best preparations contain a small amount 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.
5.4.3.2 Zn2+ enzyme-bound, occupies cobalt sites in the enzyme under conditions of insufficient cobalt in the growth medium, even the best preparations contain a small amount Clostridium sp.

Organism

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.4.3.2 additional information
-
-
 Clostridium sp.

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 required Clostridium sp.