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Ca2+
-
-
Ca2+
-
Ca2+ shows similar enhancement like Mg2+
Ca2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Ca2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Co2+
binds to enzyme
Co2+
-
can partially replace Mg2+
Co2+
a cobalt ion substitutes for Mg2+A in the crystal structure
Co2+
-
can partially replace Mg2+
Co2+
-
can partially replace Mg2+
Co2+
-
can partially replace Mg2+
Co2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Co2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
Co2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Co2+
-
can partially replace Mn2+
Mg2+
or Mn2+, required
Mg2+
-
required for maximum activity
Mg2+
-
Mg2+ enhances the enzymatic activity by increasing the affinity between UTP and the enzyme
Mg2+
strictly required. One magnesium ion catalyzes the sugar-nucleotidyl transfer reaction. 5 mM used in assay conditions
Mg2+
-
required for maximum activity
Mg2+
-
optimum activity at 3 mM
Mg2+
-
required for maximum activity
Mg2+
absolutely required, optimal concentration 20 mM
Mg2+
-
required, the enzyme utilizes two metal ions, MgA 2+ and MgB 2+, to catalyze the uridyltransfer reaction. The enzyme binds three magnesium ions and ATP at the active site. Displacement of MgB2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. In GlmUMtb[GlcNAc-1-P:ATP], the third metal ion, MgC2+ is also stabilized by one coordination interaction with Palpha and five coordination interactions with water molecules. Its coordination by Palpha results in the stabilization of an inactive conformation of ATP. Structure-function analysis, overview. The entire metal-substrate complex renders the enzyme catalytically inactive
Mg2+
required, two metal binding sites, site-A and site-B. The enzyme uses a two-metal ion mechanism (mechanism-B). Roles of the metal ions in substrate stabilization, nucleophile activation and transition-state stabilization, detailed overview. Mg2+A interacts with Asp114 and Asn239 and oxygens O1B and O2A of UDP-GlcNAc in addition to two water molecules. Mg2+B is coordinated with three water molecules and the oxygen atoms are contributed by UDP-GlcNAc and diphosphate. Mg2+A enables nucleophile activation and Mg2+B stabilizes the transition state
Mg2+
strictly required. Two magnesium ions catalyze the sugar-nucleotidyl transfer reaction. 5 mM used in assay conditions
Mg2+
-
required for maximum activity
Mg2+
-
required for maximum activity
Mg2+
-
inhibitory at high concentrations
Mg2+
-
required for maximum activity
Mg2+
-
highest activity when ratio Mg2+/diphosphate is 1/10 - 1/20
Mg2+
-
required for maximum activity
Mg2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Mg2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+. The optimal Mg2+ concentration is 6 mM, but the enzymatic activity does not change substantially between 2 and 12 mM
Mg2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Mg2+
-
can partially replace Mn2+
Mn2+
or Mg2+, required
Mn2+
or Mg2+, required. At 5 mM, 126% of the activity with Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Mn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
Mn2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
Mn2+
-
required for maximum activity, 0.5-1 mM
Ni2+
-
can partially replace Mn2+
Ni2+
-
can partially replace Mn2+
Zn2+
-
-
Zn2+
-
Zn2+ shows similar enhancement like Mg2+
Zn2+
2 mM. Activation of UDP-N-acetylglucosamine diphosphorylase activity in the order of decreasing effectiveness: Mg2+, Zn2+, Ca2+, Co2+, Mn2+. No activity is detectable without a divalent cation
Zn2+
absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+
Zn2+
no activity is detectable when a divalent cation is removed from the reaction buffer. The order of effectiveness of metal ions on GlcNAc-1-P UTase activity is Mg2+ > Zn2+ > Ca2+ > Co2+ > Mn2+, which is different from that of its Glc-1-P TTase activity, Co2+ > Mn2+ > Mg2+ > Zn2+ > Ca2+
additional information
the three-dimensional structure of the ST0452 mutant Y97N is not changed by due to lack of metals but the interactions with the substrate is slightly modified, which might cause the activity to increase
additional information
-
the three-dimensional structure of the ST0452 mutant Y97N is not changed by due to lack of metals but the interactions with the substrate is slightly modified, which might cause the activity to increase