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
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salvage
- polyamine
- adomet
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cupin
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metal-binding
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aci-reductone
-
submergence
-
deepwater
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adenosyltransferase
- methylthioribose
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phytosiderophore
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membrane-type
- mmp-2
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submergence-induced
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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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Substrates Products
Substrates Products on EC 1.13.11.54 - acireductone dioxygenase [iron(II)-requiring]
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REACTION DIAGRAM
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
1,2-dihydroxyhex-1-en-3-one + O2
2-oxopentanoate + formate
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incorporation of O2 into C1 and C2 of 1,2-dihydroxy-3-keto-1-hexene
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?
2-oxovalerate + formic acid
i.e. desthio-acireductone
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(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
2-oxovalerate + formic acid
i.e. desthio-acireductone
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?
4-(methylsulfanyl)-2-oxobutanoate + formate
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?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
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?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
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?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
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?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
A0A2V2XFM8; A0A2V2VIR7
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?
2-keto-4-methyl thiobutyrate + formate
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ir
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
2-keto-4-methyl thiobutyrate + formate
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ir
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
2-keto-4-methyl thiobutyrate + formate
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ir
3-(methylthio)propanoate + formate + CO
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?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
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?
4-(methylthio)-2-oxobutanoate + formate
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1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
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?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
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?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
enzyme of the methionine salvage pathway
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1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
Fe2+ bound to the enzyme protein. If Ni2+ or Co2+ is bound instead of Fe+, the reaction catalzed by EC 1.13.11.53 occurs instead
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1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
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ordered-sequential mechanism
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acireductone dioxygenase 1 primarily performs the on-pathway reaction with bound Fe2+ as metal cofactor. Acireductone dioxygenase 1 physically interacts with its regulator Arabidopsis thaliana G protein beta, identification of a potential Arabidopsis thaliana G protein beta-acireductone dioxygenase 1 interface, overview
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additional information
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acireductone dioxygenase 1 primarily performs the on-pathway reaction with bound Fe2+ as metal cofactor. Acireductone dioxygenase 1 physically interacts with its regulator Arabidopsis thaliana G protein beta, identification of a potential Arabidopsis thaliana G protein beta-acireductone dioxygenase 1 interface, overview
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additional information
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human ARD is capable of metal-dependent dual chemistry. The Fe2+-bound ARD shows the highest activity and catalyzes on-pathway chemistry, i.e. reaction of EC 1.13.11.54, whereas Ni2+, Co2+ or Mn2+ forms catalyze off-pathway chemistry, i.e. reasctions of EC 1.13.11.53. The enzymatic activity is metal ion cofactor dependent and the activity trend in decreasing order is Fe2+ > Ni2+ = Co2+ > Mn2+
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additional information
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OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
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additional information
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A0A2V2XFM8; A0A2V2VIR7
the enzyme has two different catalytic domains, its N-terminal half related to acireductone dioxygenase and its C-terminal half related to thioredoxin-related protein of 14 kDa. Enolase from Trypanosoma cruzi is inhibited by its interaction with metallocarboxypeptidase-1 and the enzyme
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