BRENDA - Enzyme Database show
show all sequences of 1.20.4.3

Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis

Hugo, M.; Van Laer, K.; Reyes, A.; Vertommen, D.; Messens, J.; Radi, R.; Trujillo, M.; J. Biol. Chem. 289, 5228-5239 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Mycobacterium tuberculosis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
-
-
-
Purification (Commentary)
Commentary
Organism
Ni-NTA column chromatography and Superdex 75 gel filtration
Mycobacterium tuberculosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme directly reduces the oxidized form of alkyl hydroxyperoxide reductase E, through a protein mixed disulfide with the N-terminal cysteine of mycoredoxin-1 and the sulfenic acid derivative of the peroxidatic cysteine of alkyl hydroxyperoxide reductase E
745315
Mycobacterium tuberculosis
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Mycobacterium tuberculosis
Purification (Commentary) (protein specific)
Commentary
Organism
Ni-NTA column chromatography and Superdex 75 gel filtration
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme directly reduces the oxidized form of alkyl hydroxyperoxide reductase E, through a protein mixed disulfide with the N-terminal cysteine of mycoredoxin-1 and the sulfenic acid derivative of the peroxidatic cysteine of alkyl hydroxyperoxide reductase E
745315
Mycobacterium tuberculosis
?
-
-
-
-
Other publictions for EC 1.20.4.3
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)
745091
Eberle
Biochemical and biophysical c ...
Corynebacterium pseudotuberculosis
Int. J. Biol. Macromol.
107
1999-2007
2018
-
-
1
-
-
-
8
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
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-
-
8
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
745364
Rosado
The antibacterial prodrug act ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
292
13097-13110
2017
-
-
-
-
2
-
-
-
-
-
-
-
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5
-
-
-
-
-
-
-
-
2
1
-
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-
-
-
-
2
-
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-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
741692
Si
Corynebacterium glutamicum me ...
Corynebacterium glutamicum
Appl. Environ. Microbiol.
81
2781-2796
2015
-
-
-
-
-
-
-
-
-
-
-
-
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3
-
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1
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1
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744271
Si
Functional characterization o ...
Corynebacterium glutamicum
Biochem. J.
469
45-57
2015
-
-
-
-
-
-
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-
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-
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2
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1
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1
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745315
Hugo
Mycothiol/mycoredoxin 1-depen ...
Mycobacterium tuberculosis
J. Biol. Chem.
289
5228-5239
2014
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
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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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-
-
-
-
-
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-
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-
728333
Van Laer
Mycoredoxin-1 is one of the mi ...
Mycolicibacterium smegmatis
Mol. Microbiol.
86
787-804
2012
-
-
-
1
-
-
-
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-
-
-
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5
-
1
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-
-
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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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715567
Wu
Novel channel enzyme fusion pr ...
Salinispora tropica
J. Biol. Chem.
285
40081-40087
2010
-
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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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1
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1
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2
2
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698899
Ordonez
Arsenate reductase, mycothiol, ...
Corynebacterium glutamicum
J. Biol. Chem.
284
15107-15116
2009
-
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1
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-
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1
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3
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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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