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

BRENDA support

Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.3.2 S-adenosylmethionine required Clostridium sp.
5.4.3.2 S-adenosylmethionine plays a role in lysine 2,3-aminomutase reaction Clostridium sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.3.2 Co2+ enzyme bound cofactor Clostridium sp.
5.4.3.2 Fe2+ Fe-S cluster is required as cofactor 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.
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
5.4.3.2 inactivation by purification in air, reactivation by prolonged anaerobic incubation with glutathione and dithionite 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
-
 ?

Subunits

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

Cofactor

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