BRENDA - Enzyme Database
show all sequences of 1.13.11.54

Regioselective aliphatic carbon-carbon bond cleavage by a model system of relevance to iron-containing acireductone dioxygenase

Allpress, C.J.; Grubel, K.; Szajna-Fuller, E.; Arif, A.M.; Berreau, L.M.; J. Am. Chem. Soc. 135, 659-668 (2013)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
crystal structure analysis
Klebsiella oxytoca
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on. Fe2+ transmits electrons from the residues, coordinating it to bound dioxygen and populating its formerly p*-orbital. This leads to dioxygen splitting in the second intermediate and eventual access to the Fe2+-dependent acireductone dioxygenase reaction route
Klebsiella oxytoca
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
Klebsiella oxytoca
-
4-(methylthio)-2-oxobutanoate + formate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Klebsiella oxytoca
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
-
725214
Klebsiella oxytoca
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure analysis
Klebsiella oxytoca
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on. Fe2+ transmits electrons from the residues, coordinating it to bound dioxygen and populating its formerly p*-orbital. This leads to dioxygen splitting in the second intermediate and eventual access to the Fe2+-dependent acireductone dioxygenase reaction route
Klebsiella oxytoca
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
Klebsiella oxytoca
-
4-(methylthio)-2-oxobutanoate + formate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
-
725214
Klebsiella oxytoca
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
General Information
General Information
Commentary
Organism
additional information
Fe2+-dependent acireductone dioxygenase passes through an additional split dioxygen intermediate and then proceeds through an epoxy-like transition state with a small activation energy to the two products, crystal structure analysis, structure modeling and molecular simulations of the Fe2+ and Ni2+ enzyme, cf. 1.13.11.53, QM-DMD domain, overview. The ability of Fe2+-dependent acireductone dioxygenase to stabilize an additional intermediate and thus produce the two products is due to the RedOx flexibility of the Fe2+ as compared to the more electron-rich Ni2+
Klebsiella oxytoca
physiological function
either facilitates recycling of methionine in living cells or exits this recycling pathway. Fe2+-dependent acireductone dioxygenase produces the 2-oxo acid precursor of methionine and formate
Klebsiella oxytoca
General Information (protein specific)
General Information
Commentary
Organism
additional information
Fe2+-dependent acireductone dioxygenase passes through an additional split dioxygen intermediate and then proceeds through an epoxy-like transition state with a small activation energy to the two products, crystal structure analysis, structure modeling and molecular simulations of the Fe2+ and Ni2+ enzyme, cf. 1.13.11.53, QM-DMD domain, overview. The ability of Fe2+-dependent acireductone dioxygenase to stabilize an additional intermediate and thus produce the two products is due to the RedOx flexibility of the Fe2+ as compared to the more electron-rich Ni2+
Klebsiella oxytoca
physiological function
either facilitates recycling of methionine in living cells or exits this recycling pathway. Fe2+-dependent acireductone dioxygenase produces the 2-oxo acid precursor of methionine and formate
Klebsiella oxytoca
Other publictions for EC 1.13.11.54
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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1
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742270
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Co2+ acireductone dioxygenase ...
Klebsiella oxytoca
Chem. Phys. Lett.
604
77-82
2014
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725214
Allpress
Regioselective aliphatic carbo ...
Klebsiella oxytoca
J. Am. Chem. Soc.
135
659-668
2013
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1
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2
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725438
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Acireductone dioxygenase 1 (AR ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
J. Biol. Chem.
286
30107-30118
2011
1
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1
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1
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4
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6
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1
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1
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2
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Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724
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47
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2008
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1
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9
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9
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675408
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One protein, two enzymes revis ...
Mus musculus
J. Mol. Biol.
363
823-834
2006
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1
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1
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1
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1
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1
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1
1
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663098
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Oryza sativa
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44
718-729
2005
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1
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2
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673849
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565-574
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661058
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662101
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One protein, two enzymes ...
Klebsiella oxytoca
J. Biol. Chem.
274
1193-1195
1999
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1
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2
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1
1
1
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1
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