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Fe3+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
FeSO4
the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity)
LiCl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
MnCl2
the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity)
NaCl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
NH4Cl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
Ni2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Rb+
-
enhances activity of aldolase II
Ca2+
1 mM, 82% increase of activity
Ca2+
-
can restore 10% of enzyme activity after complete inhibition by EDTA treatment (2 mM)
Cd2+
-
can partially restore activity of metal depleted enzyme
Cd2+
1 mM lowers enzyme activity by 90%
Co2+
Anacystis sp.
-
loosely bound Fe2+ or Co2+
Co2+
1 mM, 63% increase of activity
Co2+
1 mM, 128% of initial activity activity
Co2+
1 mM, 131% of initial activity activity
Co2+
-
loosely bound Fe2+ or Co2+
Co2+
-
restores activity after EDTA treatment
Co2+
-
can restore 20% of enzyme activity after complete inhibition by EDTA treatment (2 mM)
Co2+
the enzyme activity increases 2.5times in the presence of Co2+
Co2+
addition of only Co2+ and Zn2+ can recover the activity to higher than half of the original
Co2+
-
completely dependent on CoCl2. Maximal activity at 0.75 mM
Co2+
-
best divalent cation, optimal concentration: 0.2 mM
Co2+
-
better cosubstrate than Zn2+
Co2+
-
the quaternary structure reveals a tetramer composed of two dimers related by a 2-fold axis. Taq FBP aldolase subunits exhibit two distinct conformational states corresponding to loop regions that are in either open or closed position with respect to the active site. Loop closure remodels the disposition of chelating active site histidine residues. In subunits corresponding to the open conformation, the metal cofactor, Co2+, is sequestered in the active site, whereas for subunits in the closed conformation, the metal cation exchanges between two mutually exclusive binding loci, corresponding to a site at the active site surface and an interior site vicinal to the metal-binding site in the open conformation
Cu2+
1 mM lowers enzyme activity by 80%
Cu2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Fe2+
Anacystis sp.
-
loosely bound Fe2+ or Co2+
Fe2+
-
loosely bound Fe2+ or Co2+
Fe2+
-
optimum aldolase activity (137%) is observed with 1.0 mM Fe2+ concentration. Inhibition at concentrations above 1.0 mM. Activity of the enzyme completely inhibited by EDTA (2 mM) can be completely restored by Fe2+
Fe2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Fe2+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
K+
Anacystis sp.
-
stimulates
K+
1 mM, 30% increase of activity
K+
-
enhances activity of aldolase II
K+
-
the enzyme is activated up to 5.5fold by the addition of 500 mM KCl
KCl
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
KCl
-
aldolase activity increases with an increasing concentration of KCl. At 4.0 M KCl concentration, activity is 2.5 times that at 0.5 M KCl concentration. Enzyme activity is appreciable even in the absence of added salt
KCl
highest activity at 1 mM KCl
Mg2+
-
the enzyme contains four Mg2+ ions
Mg2+
-
the enzyme contains four Mg2+ ions
Mg2+
-
the enzyme contains four Mg2+ ions
Mg2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Mg2+
-
the enzyme contains four Mg2+ ions
Mg2+
contains 3 Mg2+ ions
Mg2+
the glycerone phosphate group coordinates three Mg2+ ions (Mg2Mg4)
Mg2+
-
restores activity after inhibition with EDTA
Mn2+
1 mM, 148% of inital activity
Mn2+
1 mM, 156% of inital activity
Mn2+
-
1 mM, the enzyme is dependent on Mn2+
Mn2+
-
can partially restore activity of metal depleted enzyme
Mn2+
-
restores activity after EDTA treatment
Mn2+
addition of Cu2+, Fe2+, Ni2+, Mg2+, and Mn2+ leads to only a small level of recovery of activity
Mn2+
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
Mn2+
-
restores activity after inhibition with EDTA
Na+
-
enhances activity of aldolase II
NH4+
Anacystis sp.
-
stimulates
Zn2+
1 mM, 189% increase of activity
Zn2+
-
contains 0.97 zinc atoms per subunit
Zn2+
-
the function appears to be the polarization of the C=O bound of glycerone phosphate. Each subunit of the dimer binds one Zn2+
Zn2+
-
dependent, the active site contains a zinc ion
Zn2+
FBPA belongs to the class II zinc-dependent aldolase family, each subunit contains a Zn2+ cofactor
Zn2+
-
the EDTA-inhibited activity can be restored to 109% of the original activity by the addition of 1 mM ZnSO4
Zn2+
1 mM lowers enzyme activity by 60%
Zn2+
the native recombinant enzyme is zinc-dependent, contains 0.5 Zn2+ per monomer
Zn2+
addition of only Co2+ and Zn2+ can recover the activity to higher than half of the original
Zn2+
-
contains 0.49 zinc atoms per subunit
Zn2+
-
contains 0.16 zinc atoms per subunit
Zn2+
-
contains 0.83 zinc atoms per subunit
Zn2+
can replace Co2+ at a limited rate
additional information
Anacystis sp.
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
Cd2+ has no effect on activity
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
the addition of Co2+ to the purified Bacillus cereus aldolase does not increase the relatively low specific activity of this recombinant enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
Chlamydomonas sp.
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
not dependent on Zn2+
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
1 mM Fe2+, Ca2+, or Mg2+ fail to recover the activity lost by 0.5 mM EDTA application and 0.5 mM cysteine and 1 mM 2-mercaptoethanol have almost no effect on the enzyme activity
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
Mg2+ or Ca2+ have no effect on enzme activity
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
class I fructose diphosphate aldolases, Schiff-base forming, does not require a metal ion
additional information
-
FBPasealdolase complex is located on a actinin of the Z-line. The stability of the complex is regulated by calcium ions. Elevated calcium concentration decreases association constant of FBPasealdolase and FBPase-alpha-actinin complex, causes fast dissociation of FBPase from the Z-line and slow accumulation of aldolase within the I-band and M-line. Release of Ca2+ during muscle contraction might result, simultaneously, in the inhibition of glyconeogenesis and in the acceleration of glycolysis
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
no metal requirement
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
residues involved in metal binding include Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357
additional information
-
residues involved in metal binding include Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
class I fructose diphosphate aldolases, Schiff-base forming, does not require a metal ion
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
additional information
-
Mg2+ has no effect
4.1.2.13 fructose-bisphosphate aldolase
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