4.1.1.2: oxalate decarboxylase
This is an abbreviated version!
For detailed information about oxalate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.2
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4.1.1.2
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hyperoxaluria
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velutipes
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oxalate-degrading
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flammulina
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mniii
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mn-dependent
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bicupins
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collybia
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medicine
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agriculture
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paper production
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industry
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biotechnology
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degradation
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synthesis
- 4.1.1.2
- hyperoxaluria
- velutipes
-
oxalate-degrading
-
flammulina
-
mniii
-
mn-dependent
-
bicupins
-
collybia
- medicine
- agriculture
- paper production
- industry
- biotechnology
- degradation
- synthesis
Reaction
Synonyms
AnODC, AtuOXDC, Decarboxylase, oxalate, FvOXDC, More, ODC, ODC B, ODC C, ODC E, ODC F, odc2, oxalate carboxy-lyase, oxalate-decarboxylase, oxazyme, OXD, OXDC, OxDc-CLEC, OxDcase, OxdD, pBy, TOXDC, YoaN, YvrK
ECTree
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Metals Ions
Metals Ions on EC 4.1.1.2 - oxalate decarboxylase
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Mn2+
Mn3+
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
additional information
Mn2+
contains 2 Mn2+ per subunit, role in catalysis, mechanism, 2 Mn-binding sites, the N-terminal Mn-binding site 1 is catalytically active
Mn2+
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contains Mn2+ in its resting state and two Mn-binding sites, may be only the C-terminal binding site is catalytically active, the N-terminal site not, manganese in the active site can abstract an electron from bound substrate
Mn2+
metalloenzyme, Mn2+-dependent, each cupin domain contains one Mn-binding site that is buried deeply inside the beta-barrel, 2 binding sites within a monomer, mode of binding, mechanism
Mn2+
specific requirement for the correct folding and activity, contains between 0.86 and 1.14 atoms of manganese per subunit, predominantly in the Mn2+ oxidation state, both Mn2+ and O2 are cofactors acting together as a two-electron sink during catalysis
Mn2+
required, each subunit contains two similar, but distinct, manganese sites 1 and 2, only site 1 is catalytically active, and site 2 is purely structural, manganese content of mutant enzymes, overview
Mn2+
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the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues, multifrequency EPR studies on the Mn2+ centers of oxalate decarboxylase, overview
Mn2+
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the enzyme is composed of two cupin domains, each of which contains Mn(II) coordinated by four conserved residues Arg92, Arg270, Glu162, and Glu333, the N-terminal Mn-binding site can mediate catalysis
Mn2+
two manganese binding sites, Glu162 on a flexible lid is the site 1 general acid, Mn2+ content of mutant enzymes, overview
Mn2+
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His-tagged recombinant enzyme contains 1.2 Mn2+ per subunit, non-His-tagged recombinant enzyme contains 2.0 Mn2+ per subunit
Mn2+
the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion, OxDC activity is linearly correlated with manganese content, untagged enzyme samples exhibit a metal content of 1.8 Mn2+ per monomer
Mn2+
dependent on, two Mn(II) centers located in the N- and C-terminal cupin domains of the enzyme, hydrogen bonding interaction between the side chains of a conserved Tryp132 and Glu101 coordinating Mn(II) in the N-terminal domain. Computational analysis of electronic properties of protein-bound Mn(II) ions using X-ray crystal protein structure with PDB ID 1UW8, quantum mechanical/molecular mechanical optimization and modeling, density functional theory and density functional theory/molecular mechanical calculations. Experimental and calculated fine structure parameters of wild-type and W132F mutant enzymes, overview
Mn2+
required, the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site
Mn2+
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the enzyme has two domains, each containing a Mn(II) ion coordinated with three histidine residues, binding structure in domain I, overview
enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+
additional information
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enzyme contains an additional unidentified metal binding site on the enzyme surface, modeled as Mg2+
additional information
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presence of a metal ion, role of a transition metal in catalysis