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K+
activates slightly, 10.18% activity compared to Mn2+
KCl
-
the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
NaCl
-
the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
Rb+
activates slightly, 20.67% activity compared to Mn2+
Ca2+
-
divalent metal ion is required, binding structure and conformation at the isocitrate-metal-binding site
Ca2+
-
structure of IDH1 with bound Ca2+, overview
Ca2+
activates poorly, 2.48% activity compared to Mn2+
Cd2+
-
absolute requirement for divalent cations
Cd2+
-
absolute requirement for divalent cations
Cd2+
the enzyme activity is increased at a Cd2+ concentration below 0.1 mM
Cd2+
-
absolute requirement for divalent cations
Co2+
-
absolute requirement for divalent cations
Co2+
14.3% activity compared to Mn2+
Co2+
-
absolute requirement for divalent cations
Co2+
-
absolute requirement for divalent cations
Co2+
-
can substitute for Mg2+ by 25%
Co2+
activates, 10.22% activity compared to Mn2+
Co2+
-
dependent on divalent metal ions
Co2+
activates to 43% of the activity with Mg2+
Li+
activates slightly, 12.63% activity compared to Mn2+
Li+
activates to 24% of the activity with Mg2+
Mg2+
activates
Mg2+
-
absolute requirement for divalent cations
Mg2+
5 mM used in assay conditions
Mg2+
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
69.2% activity compared to Mn2+
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
divalent cation is required, optimal activity at 40 mM in the forward reaction, and at 250 mM in the reverse reaction
Mg2+
-
2 mM used in assay conditions
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
required for activity
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
required for catalysis
Mg2+
-
divalent metal ion is required, binding structure and conformation at the isocitrate-metal-binding site
Mg2+
10 mM used in assay conditions
Mg2+
200 mM used in assay conditions
Mg2+
required for catalysis, 10 mM used in assay conditions
Mg2+
-
6 mM used in assay conditions
Mg2+
Mg2+ can partially replace the activation of Mn2+ (40.3%). 2 mM used in assay conditions
Mg2+
Mg2+ can act as a significant substitute by providing up to 58-75% of the enzyme's maximal activity
Mg2+
can partially substitute for Mn2+
Mg2+
activates, 72.45% activity compared to Mn2+
Mg2+
1 mM used in assay conditions
Mg2+
the maximum activity with Mg2+ is slightly lower than that with Cd2+
Mg2+
-
both isoforms ICD-1, ICD-2, saturation at 10 mM
Mg2+
-
absolute requirement for divalent cations
Mg2+
Pinus spp.
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
dependent on divalent metal ions, preferred metal ion
Mg2+
-
2 mM used in assay conditions
Mg2+
-
0.67 mM used in assay conditions
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
divalent cation is required, optimal activity at 2 mM in the forward reaction, and at 200 mM in the reverse reaction
Mg2+
-
requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
activates, about 50% activity compared to Mn2+, SdIDH displays a 19000-32000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+ and Mg2+, respectively
Mg2+
the recombinant IDH displays a 85000fold greater specificity for NADP+ than NAD+ with Mg2+
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
-
absolute requirement for divalent cations
Mg2+
most favorable cofactor
Mg2+
-
absolute requirement for divalent cations
Mn2+
activates
Mn2+
-
absolute requirement for divalent cations
Mn2+
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
best activating cation
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
divalent cation is required, optimal activity at 10 mM in the forward reaction, and at 50 mM in the reverse reaction
Mn2+
-
0.67 mM used in assay conditions
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
2 mM used in assay conditions
Mn2+
-
can substitute for Mg2+ by 90%
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
Km of 0.002 mM, 0.5 mM used in assay conditions
Mn2+
Mn2+ is the most favored cation, 2 mM used in assay conditions
Mn2+
Mn2+ enhances the activity the most effectively
Mn2+
activates, required, best divalent cation
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
dependent on divalent metal ions
Mn2+
-
0.67 mM used in assay conditions
Mn2+
KM-value for enzyme from normoxic heart, 0.42 mM, for enzyme from ischemic heart 0.15 mM
Mn2+
Km-value: 0.42 mM for enzyme from normoxic heart, 0.15 mM for enzyme from ischemic heart
Mn2+
-
divalent cation is required, optimal activity at 1 mM in the forward reaction, and at 20 mM in the reverse reaction
Mn2+
-
requirement for divalent cations, preferred metal ion
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
activates, preferred cation, SdIDH displays a 19000-32000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+ and Mg2+, respectively
Mn2+
the recombinant IDH displays a 62000fold (kcat/Km) preference for NADP+ over NAD+ with Mn2+
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
as Mn2+-isocitrate complex, Ser95, Asn97, and Thr78 are involved in binding
Mn2+
-
required, not bound normally
Mn2+
wild-type, Km-value 0.00033 mM
Mn2+
1 mM used in assay conditions
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
absolute requirement for divalent cations
Mn2+
activates, preferred divalent cation
Mn2+
-
absolute requirement for divalent cations
Mn2+
-
Mn2+ is the most favored divalent cation. Mn2+ can be partly replaced by Mg2+ (17.6% activity). 2 mM is used in assay conditions
Mn2+
activates to 60% of the activity with Mg2+
Mn2+
-
absolute requirement for divalent cations
Na+
-
can substitute for Mg2+ by 20%
Na+
activates slightly, 10.70% activity compared to Mn2+
Ni2+
activates poorly, 1.40% activity compared to Mn2+
Ni2+
-
absolute requirement for divalent cations
Ni2+
activates to 10% of the activity with Mg2+
Zn2+
a zinc ion is tightly bound to Asp301, Asp305, Asp277 in the active site of subunit A and subunit B
Zn2+
-
absolute requirement for divalent cations
Zn2+
-
absolute requirement for divalent cations
Zn2+
NADP+-linked activity at pH 8.5 is fully activated by the presence of Zn2+
Zn2+
activates poorly, 4.23% activity compared to Mn2+
Zn2+
-
isoform ICD-1, can replace Mg2+, saturation at 10 mM
Zn2+
-
absolute requirement for divalent cations
Zn2+
-
absolute requirement for divalent cations
additional information
the enzyme is dependent on divalent cations, overview. No activity with Zn2+, Cu2+, Ca2+, and Li+,very low activity with K+, Na+, Ni2+, and Rb+
additional information
-
K+ cannot substitute for Mg2+
additional information
Ni2+, Co2+, Na+, K+ and Li+ have almost no effect on the activity of the enzyme when assayed in the presence of Mn2+
additional information
-
the enzyme is completely divalent cation dependent. As compared with Mn2+, MaIDH shows about 2.5times and 4times higher affinities (1/Km) to NADP+ and DL-isocitrate with Mg2+, Cu2+ does not activate the enzyme at all
additional information
the enzyme is completely divalent cation dependent. As compared with Mn2+, MaIDH shows about 2.5times and 4times higher affinities (1/Km) to NADP+ and DL-isocitrate with Mg2+, Cu2+ does not activate the enzyme at all
additional information
Ca2+ does not activate Mg2+
additional information
-
no acitivty of isoforms with Mn2+ or Ca2+
additional information
the enzyme is absolutely divalent cation dependent, no or poor activation by Ca2+, Zn2+, K+, Na+, and Rb+