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Ca2+
-
the purified enzyme contains 0.39 atoms of Ca2+ per dimer
Fe2+
in heme and bound to XoxG
Ce3+
-
highest activity with 0.03 mM Ce3+. The enzyme contains 0.58 cerium atoms per subunit
Ce3+
-
lanthanide-dependent enzyme
Ce3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
Ce3+
-
the enzyme contains a cerium ion in the active site
Ce3+
-
lanthanide-dependent enzyme
Ce3+
-
remarkable activation
Ce3+
-
lanthanide-dependent enzyme
Ce3+
a lanthanide is required
Ce3+
-
lanthanide-dependent enzyme
Dy3+
-
lanthanide-dependent enzyme
Dy3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
Eu3+
-
the addition of increasing amounts of europium(III) to 200 nM purified partial-apo enzyme leads to a gradual increase in activity until saturation around 0.005 to 0.02 mM added metal is observed
Eu3+
-
lanthanide-dependent enzyme
Eu3+
-
the enzyme is dependent on the lanthanide europium
Gd3+
-
activates
Gd3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
La3+
-
second highest activity with 0.03 mM La3+
La3+
-
lanthanide-dependent enzyme
La3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
La3+
-
lanthanide-dependent enzyme
La3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
La3+
-
lanthanide-dependent enzyme
La3+
-
required, 0.03 mM used in assay conditions
La3+
lanthanides are an essential cofactor for XoxF-type methanol dehydrogenases
La3+
-
570% activity at 0.03 mM
La3+
-
dependent on. Low activity of the enzyme is detected at 0.003 mM La3+, gradually increasing with the concentration of La3+ (0.003-0.06 mM)
La3+
-
lanthanide-dependent enzyme
La3+
-
activates, 0.002 mM used in assay conditions
La3+
-
dependent on. XoxF1 contains La3+ in 1:1 molar ratio of metal to protomer
La3+
-
the enzyme is activated by La3+. The purified enzyme contains 0.91 atoms of La3+ atoms per dimer
La3+
the enzyme preferentially binds La3+ over Ca2+ in the active site. 0.1 mM used in assay conditions. The enzyme contains 1.3 mol of La3+ per mol of protomer
La3+
a lanthanide is required
La3+
-
lanthanide-dependent enzyme
La3+
lanthanide-dependent enzyme
La3+
lanthanide-dependent enzyme. Although La3+ and Nd3+ have similar distributions in nature, XoxF can chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme
La3+
-
lanthanide-dependent enzyme
La3+
-
required for activity
La3+
-
contains a La3+ ion in the active site
La3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
La3+
lanthanide-dependent enzyme
La3+
-
lanthanide-dependent enzyme
La3+
-
lanthanide-dependent enzyme
La3+
-
lanthanide-dependent enzyme
Lu3+
-
lanthanide-dependent enzyme
Lu3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
Nd3+
-
activates at 0.03 mM
Nd3+
-
lanthanide-dependent enzyme
Nd3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Nd3+
a lanthanide is required
Nd3+
-
lanthanide-dependent enzyme
Nd3+
lanthanide-dependent enzyme
Nd3+
lanthanide-dependent enzyme. Although La3+ and Nd3+ have similar distributions in nature, XoxF can chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme
Nd3+
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Pr3+
-
activates at 0.03 mM
Pr3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
Pr3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
Pr3+
-
lanthanide-dependent enzyme
Sm3+
-
slight activation
Sm3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
additional information
-
the enzyme does not require ammonium ions for activation
additional information
-
the enzyme is completely independent of ammonium
additional information
-
not activated by Ca2+
additional information
-
the enzyme has a requirement for ammonia
additional information
-
the enzyme preferentially uses lanthanides over calcium even when lanthanides are present at a 10fold-lower concentration
additional information
lanthanides, especially the lighter and most abundant members (La, Ce, Pr, Nd, Sm, and Eu) of the lanthanide (Ln) series, are essential for catalysis in the most broadly distributed class of pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenases (MDHs). The number of distinct lanthanides supporting catalysis in vitro and/or in vivo differs from enzyme to enzyme: e.g. La-Nd, La-Sm/Eu, or La-Gd, according to the XoxF clade, in which an enzyme is found. Strain AM1 XoxF1 can be activated in vivo with La, Ce, Pr, and Nd, and poorly or not at all with Sm. The lanthanides are incorporated when they are added individually to the growth media, XoxF expressed in the presence of La, either from endogenous levels or recombinantly in a methylotroph, show roughly stoichiometric La incorporation, Nd incorporation is more variable. By contrast, plasmid-based expression of XoxF in the presence of Nd leads to substoichiometric Nd insertion into XoxF
additional information
-
XoxF has maximal activity in the standard artificial dye-linked assay when metallated with Pr and Nd. Activity is about 30% lower with La and falls off quickly beyond Nd. This biphasic behavior is attributed to competition between the Lewis acidity of the LnIII ion, increasing across the series and therefore enhancing reactivity of the pyrroloquinoline quinone (PQQ) cofactor, with other, opposing factors
additional information
XoxF has maximal activity in the standard artificial dye-linked assay when metallated with Pr and Nd. Activity is about 30% lower with La and falls off quickly beyond Nd. This biphasic behavior is attributed to competition between the Lewis acidity of the LnIII ion, increasing across the series and therefore enhancing reactivity of the pyrroloquinoline quinone (PQQ) cofactor, with other, opposing factors
additional information
-
subtype XoxF4-1 can use lighter lanthanides up to the atomic number of 64 (La3+ through Gd3+) while subtype XoxF4-2 can only use lanthanides up to the atomic number of 62 (La3+ through Sm3+)