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Ni2+
-
divalent metal ion required, NADP+-linked activity exhibits a maximum at 5 mM Ni2+
Zn2+
5fold activation at 5 mM, only slight activation at 10 mM
Co2+
-
can replace Mg2+ in activation. Km: 0.018 mM
Co2+
activates 7fold at 1-10 mM
Mg2+
Amaranthus edulis
-
no activation by Mg2+
Mg2+
a divalent metal ion, Mn+2 or Mg+2+, is essential for the enzyme reaction
Mg2+
-
no activation by Mg2+
Mg2+
-
strict requirement for a divalent cation, maximal activation at 2 mM
Mg2+
-
no decarboxylation of malate in absence of either Mg2+ or NAD+. Km: 0.04 mM
Mg2+
-
divalent metal ion required, NAD+-linked activity shows maximal activity at 5 mM Mg2+
Mg2+
Crassula argentea
-
activation by Mg2+ or Mn2+
Mg2+
Crassula argentea
-
uses Mg2+ or Mn2+ as the required divalent cation
Mg2+
-
completely dependent on the presence of Mg2+ or Mn2+
Mg2+
-
Mn2+ or Mg2+ required
Mg2+
-
Km with NAD+: 4.25 mM, Km with NADP+: 13.3 mM
Mg2+
-
no activation by Mg2+
Mg2+
-
bivalent metal ion required, Mn2+ is more effective than Mg2+
Mg2+
activates 12fold at 1 mM and 15fold at 10 mM
Mg2+
-
activation by Mg2+ or Mn2+
Mg2+
-
activation by Mn2+, at 1 mM, is 10% and 20% higher than activation with 1 mM Mg2+ in the presence of NAD+ and NADP+
Mg2+
-
completely dependent on the presence of Mg2+ or Mn2+
Mg2+
-
preferably used as metal cofactor
Mn2+
-
activates the enzyme in mitochondria, kinetics, overview
Mn2+
Amaranthus edulis
-
absolute requirement for Mn2+, no activation by Mg2+
Mn2+
a divalent metal ion, Mn+2 or Mg+2+, is essential for the enzyme reaction
Mn2+
-
activates mutant N434A
Mn2+
-
absolute requirement for Mn2+, no activation by Mg2+
Mn2+
-
strict requirement for a divalent cation, maximal activation at 5 mM
Mn2+
-
can replace Mg2+ in activation
Mn2+
-
10 mM used in assay conditions
Mn2+
-
activates, Km 0.08 mM in the decarboxylation/oxidation reaction
Mn2+
-
activates, Km is 0.08 mM
Mn2+
Crassula argentea
-
divalent cation required, Mg2+ or Mn2+
Mn2+
Crassula argentea
-
activation by Mn2+ or Mg2+
Mn2+
-
completely dependent on the presence of Mg2+ or Mn2+
Mn2+
-
reversible structural interconversion to the Lu3+-binding form, metal binding site structure
Mn2+
-
during the catalytic process of malic enzyme, binding of metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form
Mn2+
Mnium undulatum
-
activates
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
Km with NAD+: 0.14 mM, Km with NADP+: 0.81 mM
Mn2+
-
absolute requirement for Mn2+, no activation by Mg2+
Mn2+
-
bivalent metal ion required, Mn2+ is more effective than Mg2+
Mn2+
activates 13fold at 1 mM and 15fold at 10 mM
Mn2+
-
activation by Mn2+ or Mg2+
Mn2+
-
completely dependent on the presence of Mg2+ or Mn2+
Mn2+
-
activates, 5 mM used in assay conditions
NH4+
-
partially rescues the activity of the R181Q mutant by binding in the pocket vacated by the guanidinium group of R181, 2 mol of ammonia bind per mole of active sites, high-affinity Km is 0.7 mM, low-affinity Km is 420 mM
NH4+
activates 12fold at 1 mM and 20fold at 10 mM
additional information
-
the reaction is dependent on divalent metal ions
additional information
malic enzyme activity is markedly enhanced by mono- and divalent cations