1.1.1.267 Ca2+ activates, a divalent cation is required for activity, can partially substitute for Mn2+ 676660 1.1.1.267 Co2+ activates, a divalent cation is required for activity, can partially substitute for Mn2+ 676660 1.1.1.267 Co2+ can partially substitute for Mg2+ or Mn2+ 724543, 725564 1.1.1.267 Co2+ required for activity 286427, 286428 1.1.1.267 Co2+ required, Km-value 0.001 mM 654877 1.1.1.267 Co2+ required, Km-value 0.0012 mM 654748 1.1.1.267 Mg2+ - 697335 1.1.1.267 Mg2+ a divalent cation is absolutely required, optimal at 10 mM, the enzyme prefers Mn2+ or Mg2+ 673562 1.1.1.267 Mg2+ a divalent metal ion is absolutely required for activity, involved in catalysis 672538 1.1.1.267 Mg2+ absolutely dependent on, optimal at 4 mM 674260 1.1.1.267 Mg2+ activates 672040, 724374, 762747 1.1.1.267 Mg2+ activates, a divalent cation is required for activity, can partially substitute for Mn2+ 676660 1.1.1.267 Mg2+ activates, can substitute for Mg2+ 723812 1.1.1.267 Mg2+ active site divalent metal ion 763000 1.1.1.267 Mg2+ can partly substitute for Co2+, Km-value 1.2 mM 654748 1.1.1.267 Mg2+ complex with 286423 1.1.1.267 Mg2+ Km-value 2.37 mM 654877 1.1.1.267 Mg2+ Mg2+ is prefered over Mn2+ 712892 1.1.1.267 Mg2+ or Mn2+, required 655439 1.1.1.267 Mg2+ required 675580, 720429, 724346, 724558, 725663, 760333, 762667, 762794, 763591 1.1.1.267 Mg2+ required for activity 286427, 286428 1.1.1.267 Mg2+ the enzyme essentially requires Mg2+ or Mn2+ 724543, 725564 1.1.1.267 Mg2+ the enzyme requires divalent metal ions 675038 1.1.1.267 Mg2+ the enzyme requires the presence of a divalent metal ion for activity 763482 1.1.1.267 Mn2+ - 697335 1.1.1.267 Mn2+ a divalent cation is absolutely required, the enzyme prefers Mn2+ or Mg2+ 673562 1.1.1.267 Mn2+ a divalent metal ion is absolutely required for activity, involved in catalysis 672538 1.1.1.267 Mn2+ activates 762747 1.1.1.267 Mn2+ activates, a divalent cation is required for activity, best cation, can partially be substituted by other divalent cations 676660 1.1.1.267 Mn2+ active site divalent metal ion 763000 1.1.1.267 Mn2+ bound to the enzymes' active site 673073 1.1.1.267 Mn2+ can poorly replace for Co2+, Km-value 2.4 mM 654748 1.1.1.267 Mn2+ may substitute for Co2+, Km-value 0.0015 mM 654877 1.1.1.267 Mn2+ Mg2+ is prefered over Mn2+ 712892 1.1.1.267 Mn2+ or Mg2+, required 655439 1.1.1.267 Mn2+ required 671075, 671590, 763279 1.1.1.267 Mn2+ required for activity 286427, 286428, 672396 1.1.1.267 Mn2+ required, activates 723812 1.1.1.267 Mn2+ the enzyme essentially requires Mg2+ or Mn2+ 724543, 725564 1.1.1.267 Mn2+ the enzyme requires divalent metal ions 675038 1.1.1.267 additional information divalent cation is required 712892 1.1.1.267 additional information divalent cations required for acitvity, activity decreases in the following order: Co2+, Mn2+, Mg2+, Ba2+, Ca2+, Cu2+ 286424 1.1.1.267 additional information Dxrs require a divalent metal for their activity. The enzymes may use Mg2+ or Mn2+ cations. The enzyme forms a dimeric assembly and contains a metal ion in the active site. The residues coordinating the metal are parts of two highly conserved protein fragments: 148-PVDSEHXA-155 and 227-NKGLEXIE-234. The first of these fragments is bridging the N- and C-terminal domains. Residues E152 and E231 are the major residues involved in metal binding, and in three crystal structure cases they are the only amino acids involved in interactions with the metal. In the fourth case the metal ion is coordinated by D150, E152 and E231 (PDB ID 5KRR, chain B) 762747 1.1.1.267 additional information Mn2+, Ca2+, Co2+, Zn2+, and Fe2+ ions are unable to support activity 674260 1.1.1.267 additional information no activity with Fe2+ and Cu2+ 676660 1.1.1.267 phosphite dianion activation by phosphite dianion 724374 1.1.1.267 Zn2+ activates, a divalent cation is required for activity, can partially substitute for Mn2+ 676660