Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.3.2 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
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+ enzyme bound cofactor 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.

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium sp.

Reaction

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

Cofactor

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