1.13.11.54: acireductone dioxygenase [iron(II)-requiring]
This is an abbreviated version!
For detailed information about acireductone dioxygenase [iron(II)-requiring], go to the full flat file.
Word Map on EC 1.13.11.54
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1.13.11.54
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metalloproteinase
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ethylene
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s-adenosylmethionine
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mt1-mmp
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mta
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salvage
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polyamine
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adomet
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cupin
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metal-binding
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aci-reductone
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submergence
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deepwater
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adenosyltransferase
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methylthioribose
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phytosiderophore
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membrane-type
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mmp-2
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submergence-induced
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mt1-mmp-mediated
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medicine
- 1.13.11.54
- metalloproteinase
- ethylene
- s-adenosylmethionine
- mt1-mmp
- mta
-
salvage
- polyamine
- adomet
-
cupin
-
metal-binding
-
aci-reductone
-
submergence
-
deepwater
-
adenosyltransferase
- methylthioribose
-
phytosiderophore
-
membrane-type
- mmp-2
-
submergence-induced
-
mt1-mmp-mediated
- medicine
Reaction
Synonyms
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, aci-reductone dioxygenase, acireductone dioxygenase, acireductone dioxygenase 1, ADI1, ARD, ARD', ARD1, ARD4, ARDp, Fe(II)-bound acireductone dioxygenase, Fe-ARD, MTCBP-1, MtnD, OsARD1, Ymr009p
ECTree
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Engineering
Engineering on EC 1.13.11.54 - acireductone dioxygenase [iron(II)-requiring]
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E100A
about 2% of wild-type activity. E100 is not essential for metal binding
H98S
no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals
E100A
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about 2% of wild-type activity. E100 is not essential for metal binding
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H98S
E91A
additional information
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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
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H98S
mutation results in the formation of a stable soluble protein that while structurally different from ARD shows a high degree of similarity to the ARD' enzyme
usage of three tDNA insertion mutant alleles, ard1-1 (SALK_119327), ard1-2 (GABI_595C04), and ard1-3 (SALK_034308).
additional information
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usage of three tDNA insertion mutant alleles, ard1-1 (SALK_119327), ard1-2 (GABI_595C04), and ard1-3 (SALK_034308).
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