BRENDA - Enzyme Database show
show all sequences of 1.20.4.3

Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange

Ordonez, E.; Van Belle, K.; Roos, G.; De Galan, S.; Letek, M.; Gil, J.A.; Wyns, L.; Mateos, L.M.; Messens, J.; J. Biol. Chem. 284, 15107-15116 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arseno-mycothiol + mycoredoxin
Corynebacterium glutamicum
reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by arsenate-mycothiol transferase. A second mycothiol recycles mycoredoxin and forms mycothione
arsenite + mycothiol-mycoredoxin disulfide
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
-
-
-
Purification (Commentary)
Commentary
Organism
-
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arseno-mycothiol + mycoredoxin
-
698899
Corynebacterium glutamicum
arsenite + mycothiol-mycoredoxin disulfide
a second mycothiol recycles mycoredoxin and forms mycothione
-
-
?
arseno-mycothiol + mycoredoxin
reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by arsenate-mycothiol transferase. A second mycothiol recycles mycoredoxin and forms mycothione
698899
Corynebacterium glutamicum
arsenite + mycothiol-mycoredoxin disulfide
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arseno-mycothiol + mycoredoxin
Corynebacterium glutamicum
reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by arsenate-mycothiol transferase. A second mycothiol recycles mycoredoxin and forms mycothione
arsenite + mycothiol-mycoredoxin disulfide
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arseno-mycothiol + mycoredoxin
-
698899
Corynebacterium glutamicum
arsenite + mycothiol-mycoredoxin disulfide
a second mycothiol recycles mycoredoxin and forms mycothione
-
-
?
arseno-mycothiol + mycoredoxin
reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by arsenate-mycothiol transferase. A second mycothiol recycles mycoredoxin and forms mycothione
698899
Corynebacterium glutamicum
arsenite + mycothiol-mycoredoxin disulfide
-
-
-
?
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
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1
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8
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2
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1
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1
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1
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8
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1
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1
1
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1
1
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745364
Rosado
The antibacterial prodrug act ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
292
13097-13110
2017
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2
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5
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2
1
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1
1
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741692
Si
Corynebacterium glutamicum me ...
Corynebacterium glutamicum
Appl. Environ. Microbiol.
81
2781-2796
2015
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3
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744271
Si
Functional characterization o ...
Corynebacterium glutamicum
Biochem. J.
469
45-57
2015
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745315
Hugo
Mycothiol/mycoredoxin 1-depen ...
Mycobacterium tuberculosis
J. Biol. Chem.
289
5228-5239
2014
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1
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3
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1
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1
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728333
Van Laer
Mycoredoxin-1 is one of the mi ...
Mycolicibacterium smegmatis
Mol. Microbiol.
86
787-804
2012
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1
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5
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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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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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1
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3
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1
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