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

BRENDA support

Literature summary for 5.4.3.2 extracted from

  • Frey, P.A.; Moss, M.; Petrovich, R.; Baraniak, J.
    The roles of S-adenosylmethionine and pyridoxal phosphate in the lysine 2,3-aminomutase reaction (1990), Ann. N. Y. Acad. Sci., 585, 368-378.
    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.
S-adenosylmethionine plays a role in lysine 2,3-aminomutase reaction 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.

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-

Oxidation Stability

Oxidation Stability Organism
inactivation by purification in air, reactivation by prolonged anaerobic incubation with glutathione and dithionite Clostridium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Lys
-
 Clostridium sp. (3S)-3,6-diaminohexanoic acid
-
 ?

Subunits

Subunits Comment Organism
hexamer gel filtration Clostridium sp.
hexamer 6 * 48000, SDS-PAGE Clostridium sp.

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required Clostridium sp.
pyridoxal 5'-phosphate role in lysine 2,3-aminomutase reaction Clostridium sp.