Ligand Mn3+

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Basic Ligand Information

Molecular Structure
Picture of Mn3+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Mn
Mn3+
MMIPFLVOWGHZQD-UHFFFAOYSA-N
Synonyms:
Manganese(3+), manganese(III), Mn(III)
Pathway Source
Pathways

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
Mn3+ + O2 + H2O = MnIVO2 + H+
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In Vivo Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
Mn2+ + H+ + H2O2 = Mn3+ + H2O
-
-
show the reaction diagram
Mn2+ + O2 + H+ = Mn3+ + H2O
-

Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
Mn3+ + O2 + H2O = MnIVO2 + H+
-

Product in Enzyme-catalyzed Reactions (9 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
Mn2+ + O2 + H+ = Mn3+ + H2O
-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
Mn3+ has 30-60% of the specific activity of Fe3+-CBS
-
1 mM, 8% residual activity
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Metals and Ions (50 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
substitution of ferric heme by MnIII protoporphyrin IX greatly diminishes the peroxidase activity, but has little effect on the cyclooxygenase activity
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the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
dimanganese(III)-tyrosyl radical cofactor
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
dimanganese(III)-tyrosyl radical cofactor
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
treatment of the periodate-oxidized enzyme with ascorbate results in a substantioal decrease in absorption, forming a complex that is spectroscopically identified as a Mn3+ species. Mn3+ form has a 5fold higher specific activity than native recombinant oxalate oxidase.
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enzyme contains one atom of Mn(III) per 110000 Da enzyme
-
Mn3+ may play an important role on effective binding of phosphate and acceleration of hydrolysis of phosphomonoesters at pH 4-6
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required for activity. Up to 16% of the electron paramagnetic resonance-visible manganese is in the +3 oxidation state at low pH in the presence of succinate buffer
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3D Structure of Enzyme-Ligand-Complex (PDB) (118 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

References & Links

Links to other databases for Mn3+

ChEBI
PubChem
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PubChem