1.13.11.53: acireductone dioxygenase (Ni2+-requiring)
This is an abbreviated version!
For detailed information about acireductone dioxygenase (Ni2+-requiring), go to the full flat file.
Word Map on EC 1.13.11.53
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1.13.11.53
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salvage
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monoxide
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cupins
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mta
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on-pathway
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oxytoca
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nickel-containing
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ketoacid
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ni2+-containing
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membrane-type
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submergence-induced
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nickel-dependent
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nickelii
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nife-hydrogenase
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benzil
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2-keto-4-methylthiobutyrate
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ch3cn
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metallocenters
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analysis
- 1.13.11.53
-
salvage
- monoxide
-
cupins
- mta
-
on-pathway
- oxytoca
-
nickel-containing
-
ketoacid
-
ni2+-containing
-
membrane-type
-
submergence-induced
-
nickel-dependent
-
nickelii
- nife-hydrogenase
- benzil
- 2-keto-4-methylthiobutyrate
- ch3cn
-
metallocenters
- analysis
Reaction
Synonyms
2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase, aci-reductone dioxygenase, acidoreductone dioxygenase, acireductone dioxygenase, acireductone dioxygenase 1, ADI1, ARD, ARD1, human aci-reductone dioxygenase 1, membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1, MTCBP1, MtnD, Ni(II)-ARD, Ni(II)-bound acireductone dioxygenase, Ni-ARD, nickel acireductone dioxyegenase, nickel acireductone dioxygenase, Sip-L
ECTree
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Metals Ions
Metals Ions on EC 1.13.11.53 - acireductone dioxygenase (Ni2+-requiring)
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Co2+
Iron
the enzyme contains a non-heme, iron-binding site critical for its activity
Mn2+
Ni2+
Nickel
additional information
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the identity of bound metal ion does not affect the oligomeric state of ARD
Co2+
quantum-classical dynamics simulations with Co2+ bound. both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD, but the mechanism involves a bifurcating transition state, and so the exact product distribution is determined by the reaction dynamics
Co2+
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apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule
Co2+
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Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Mn2+
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Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Ni2+
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apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule
Ni2+
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solution structure of the nickel-containing enzyme is determined using NMR methods. X-ray absorption spectroscopy, assignment of hyperfine shifted NMR resonance and conserved domain homology are used to model the metal-binding site because of the paramagnetism of the bound Ni2+
Ni2+
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structure of the Ni site in resting Ni-ARD as containing a six coordinate Ni site composed of O/N-donor ligands including 3-4 histidine residues. The substrate binds to the Ni center in a bidentate fashion by displacing two ligands, at least one of which is a histidine ligand
Ni2+
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model for the solution structure of the paramagnetic Ni2+-containing enzyme
Ni2+
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Ni2+ can be conservatively replaced by Mn2 +or Co2+, giving rise to ARD activity (CO production)
Ni2+
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Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
detection of one-bond 15N-13Calpha correlations in the vicinity of the paramagnetic Ni2+
Nickel
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ligands are H96, H98, E102 and H140, the same as in the isoform requiring Fe2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions