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Co2+
-
the reaction requires a divalent metal ion
Mg2+
required
Mg2+
the enzyme utilizes Mg2+ in the enzyme catalysis
Mg2+
-
Km: 0.4 mM, pH 8.5
Mg2+
-
Km: 0.35 mM, pH 10, reaction with acetolactate
Mg2+
-
Km: 0.45 mM, pH 6.7, reaction with acetolactate
Mg2+
-
with acetolactate as substrate , Mg2+ is the only divalent metal ion that supports enzyme catalysis
Mg2+
-
the reaction requires a divalent metal ion
Mg2+
the coordination geometry for Mg(1) is approximately octahedral, with three water ligands and three protein ligands, the carboxylate groups of D217, E389 and E393. Mg(2) is seven coordinate with six waters and a carboxylate oxygen from D217. A dissociation constant of about 500 microM applies to the interaction of Mg2+ with unliganded enzyme. In presence of NADPH the Kd increases to about 800 microM
Mg2+
two magnesium ions are located deep in the active site pocket and are separated by 4.7 A. The side chains of D188 and E192, and four water molecules form ligands with one of the Mg2+ ions, Mg2+(I), and the second Mg2+ ion, Mg2+ (II), is liganded also by the side-chain of D188, in addition to E224 and E228 and three water molecules
Mg2+
-
optimum concentration 5 mM
Mg2+
required, KM: 0.00324 mM
Mg2+
-
required for the alkyl migration reaction step
Mg2+
required for the alkyl migration reaction, Km is 0.0072 mM, binding structure, overview
Mg2+
-
Km for Mg2+: 0.0045 mM, at pH 8.2, 30°C
Mg2+
-
two ions bind to enzyme
Mg2+
two ions bind to enzyme
Mg2+
Mg2+-dependent enzyme
Mg2+
active site contains two divalent Mg2+ cations
Mg2+
the enzyme binds two Mg2+ ions in the active site to bridge the substrate ligand and protein. The substrate binding and catalytic efficiency of KARI are highly dependent on the Mg2+ concentration
Mn2+
-
activates reaction with 3-hydroxy-3-methyl-2-oxobutanoate, no effect on reaction with acetolactate
Mn2+
-
the reaction requires a divalent metal ion
additional information
-
Mn2+, Co2+, Ni2+, Zn2+, Ca2+, Cu2+ and Co3+ can not substitute for Mg2+
additional information
-
Mn2+, Co2+, Ni2+, Zn2+, Ca2+, Cu2+ and Co3+ can not substitute for Mg2+
additional information
-
metal ions other than Mg2+ are inhibitory
additional information
the enzyme catalyzes a two-step reaction: an alkyl migration that requires Mg2+, and a reduction reaction involving NADPH. For the reduction reaction, a divalent metal ion is also required, with any of Mg2+, Mn2+, Co2+, or Ni2+ utilized in this role
additional information
-
the enzyme catalyzes a two-step reaction: an alkyl migration that requires Mg2+, and a reduction reaction involving NADPH. For the reduction reaction, a divalent metal ion is also required, with any of Mg2+, Mn2+, Co2+, or Ni2+ utilized in this role
additional information
-
the NADPH reaction step requires a divalent cation, e.g. Mg2+, Mn2+, or Co2+, but in a non-specific manner
additional information
-
no metal ions required
additional information
-
no metal ions required