BRENDA - Enzyme Database
show all sequences of 1.13.11.54

One protein, two enzymes

Dai, Y.; Wensink, P.C.; Abeles, R.H.; J. Biol. Chem. 274, 1193-1195 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Klebsiella oxytoca
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
210
-
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one
-
Klebsiella oxytoca
210
-
O2
-
Klebsiella oxytoca
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
apoenzyme is catalytically inactive. Addition of Fe2+ yields activity. Production of the enzyme in intact Escherichia coli depends on the availability of the Fe2+. Enzyme contains 0.9 Fe2+ per enzyme molecule
Klebsiella oxytoca
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
20240
-
mass spectrometry
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
enzyme of the methionine salvage pathway
4-(methylthio)-2-oxobutanoate + formate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Klebsiella oxytoca
Q9ZFE7
-
-
Purification (Commentary)
Commentary
Organism
recombinant
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
enzyme of the methionine salvage pathway
662101
Klebsiella oxytoca
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
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
662101
Klebsiella oxytoca
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Klebsiella oxytoca
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
210
-
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one
-
Klebsiella oxytoca
210
-
O2
-
Klebsiella oxytoca
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
apoenzyme is catalytically inactive. Addition of Fe2+ yields activity. Production of the enzyme in intact Escherichia coli depends on the availability of the Fe2+. Enzyme contains 0.9 Fe2+ per enzyme molecule
Klebsiella oxytoca
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
20240
-
mass spectrometry
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
enzyme of the methionine salvage pathway
4-(methylthio)-2-oxobutanoate + formate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant
Klebsiella oxytoca
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
enzyme of the methionine salvage pathway
662101
Klebsiella oxytoca
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
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
662101
Klebsiella oxytoca
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
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)
743725
Deshpande
Dual chemistry catalyzed by h ...
Homo sapiens
Protein Eng. Des. Sel.
30
197-204
2017
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1
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1
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1
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2
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1
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1
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1
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2
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1
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-
741923
Deshpande
Metal-dependent function of a ...
Mus musculus
Biochemistry
55
1398-1407
2016
-
-
-
1
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-
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1
-
5
1
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1
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1
1
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2
1
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1
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1
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5
1
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1
1
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2
1
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1
1
743184
Chang
Interaction between hepatic m ...
Homo sapiens
J. Viral Hepat.
23
256-266
2016
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1
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1
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3
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1
1
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742270
Valdez
-
Co2+ acireductone dioxygenase ...
Klebsiella oxytoca
Chem. Phys. Lett.
604
77-82
2014
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1
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1
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1
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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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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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2
2
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725438
Friedman
Acireductone dioxygenase 1 (AR ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
J. Biol. Chem.
286
30107-30118
2011
1
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1
-
1
-
-
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-
1
-
4
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6
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1
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4
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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4
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1
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4
1
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2
2
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-
685212
Chai
Characterization of metal bind ...
Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724
Biochemistry
47
2428-2438
2008
-
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1
-
9
-
-
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1
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2
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1
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9
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1
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675408
Ju
One protein, two enzymes revis ...
Mus musculus
J. Mol. Biol.
363
823-834
2006
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1
-
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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1
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1
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1
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1
1
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663098
Sauter
The immediate-early ethylene r ...
Oryza sativa
Plant J.
44
718-729
2005
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1
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2
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1
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1
-
2
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1
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2
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2
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2
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1
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2
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1
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1
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1
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2
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2
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2
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673849
Hirano
Membrane-type 1 matrix metallo ...
Homo sapiens, Saccharomyces cerevisiae, Saccharomyces cerevisiae Y700
Genes Cells
10
565-574
2005
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2
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4
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3
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2
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3
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661058
Dai
Mechanistic studies of two dio ...
Klebsiella pneumoniae
Biochemistry
40
6379-6387
2001
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2
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1
2
1
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1
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1
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3
1
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2
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2
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1
2
1
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1
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3
1
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2
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662101
Dai
One protein, two enzymes ...
Klebsiella oxytoca
J. Biol. Chem.
274
1193-1195
1999
-
-
1
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-
-
2
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1
1
1
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1
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1
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2
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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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2
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