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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Engineering
Engineering on EC 1.13.11.53 - acireductone dioxygenase (Ni2+-requiring)
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E94A
H133A
the mutation at the metal-binding site abolishes both functions of the enzyme in cell growth inhibition and apoptosis enhancement
E100A
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about 2% of wild-type activity. E100 is not essential for metal binding
H98S
E94A
the mutant has an increased percentage of apoptotic cells similar to those expressing wild type enzyme
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no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals
H98S
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mutation results in the formation of a stable soluble protein that while structurally different from ARD-Ni+2 shows a high degree of similarity to the ARD'(Fe) enzyme