4.2.1.19 Mg2+ metalloprotein, transition metals induce aggregation and are required for catalysis, 1 equivalent of Mn2+ per subunit induces the formation of 24-mers from the trimeric enzyme 652527 4.2.1.19 Mn the manganese cluster is critical in converting the inactive trimeric state of the enzyme into its biologically active 24-mer and also forms the active site. The substrate is bound to the manganese cluster as an imidazole moiety that subsequently collapse to yield a diazafulvene intermediate 666944 4.2.1.19 Mn2+ 0.5 mM enhances the activity 7fold 5540 4.2.1.19 Mn2+ activity dependent on 5533 4.2.1.19 Mn2+ contains two Mn2+ ions, 0.05 mM Mn2+ used in assay conditions 728872 4.2.1.19 Mn2+ essential for assembly of subunits 5546 4.2.1.19 Mn2+ Km: 0.0073 mM 5535 4.2.1.19 Mn2+ Km: 0.0076 mM 5534 4.2.1.19 additional information not activated by Mg2+, Ni2+, Cd2+, Fe2+, Co2+ 5538 4.2.1.19 additional information not activated by Mg2+, Ni2+, Cd2+, Fe2+, Co2+, Fe3+ 5540