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Literature summary for 5.4.3.2 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
Search for more literature for 5.4.3.2

Activating Compound

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ contains 3.5 gatom of cobalt per mol of enzyme Clostridium sp.
Co2+ enzyme bound cofactor Clostridium sp.
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.
Fe2+ Fe-S cluster is required as cofactor Clostridium sp.
Fe2+ 12 gatom of iron and of sulfide per mol of hexameric enzyme Clostridium sp.
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

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

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium sp.

Specific Activity [micromol/min/mg]

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

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 required Clostridium sp.