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Ca2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
phosphite dianion
-
activation by phosphite dianion
Zn2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
Co2+
-
required for activity
Co2+
required for activity
Co2+
-
can partially substitute for Mg2+ or Mn2+
Co2+
-
required, Km-value 0.0012 mM
Co2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
Co2+
-
required, Km-value 0.001 mM
Co2+
-
can partially substitute for Mg2+ or Mn2+
Mg2+
a divalent cation is absolutely required, optimal at 10 mM, the enzyme prefers Mn2+ or Mg2+
Mg2+
-
required for activity
Mg2+
required for activity
Mg2+
-
activates, can substitute for Mg2+
Mg2+
active site divalent metal ion
Mg2+
the enzyme requires the presence of a divalent metal ion for activity
Mg2+
-
can partly substitute for Co2+, Km-value 1.2 mM
Mg2+
-
absolutely dependent on, optimal at 4 mM
Mg2+
-
the enzyme essentially requires Mg2+ or Mn2+
Mg2+
active site divalent metal ion
Mg2+
activates, can substitute for Mg2+
Mg2+
the enzyme requires divalent metal ions
Mg2+
active site divalent metal ion
Mg2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
Mg2+
-
a divalent metal ion is absolutely required for activity, involved in catalysis
Mg2+
Mg2+ is prefered over Mn2+
Mg2+
-
the enzyme essentially requires Mg2+ or Mn2+
Mn2+
a divalent cation is absolutely required, the enzyme prefers Mn2+ or Mg2+
Mn2+
-
required for activity
Mn2+
required for activity
Mn2+
bound to the enzymes' active site
Mn2+
-
required, activates
Mn2+
active site divalent metal ion
Mn2+
-
can poorly replace for Co2+, Km-value 2.4 mM
Mn2+
-
the enzyme essentially requires Mg2+ or Mn2+
Mn2+
active site divalent metal ion
Mn2+
the enzyme requires divalent metal ions
Mn2+
active site divalent metal ion
Mn2+
activates, a divalent cation is required for activity, best cation, can partially be substituted by other divalent cations
Mn2+
-
required for activity
Mn2+
-
may substitute for Co2+, Km-value 0.0015 mM
Mn2+
-
a divalent metal ion is absolutely required for activity, involved in catalysis
Mn2+
Mg2+ is prefered over Mn2+
Mn2+
-
the enzyme essentially requires Mg2+ or Mn2+
additional information
-
Mn2+, Ca2+, Co2+, Zn2+, and Fe2+ ions are unable to support activity
additional information
no activity with Fe2+ and Cu2+
additional information
divalent cation is required
additional information
-
divalent cation is required
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)
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)
additional information
-
divalent cations required for acitvity, activity decreases in the following order: Co2+, Mn2+, Mg2+, Ba2+, Ca2+, Cu2+