Information on EC 1.20.4.3 - mycoredoxin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.20.4.3
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RECOMMENDED NAME
GeneOntology No.
mycoredoxin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
arseno-mycothiol + mycoredoxin = arsenite + mycothiol-mycoredoxin disulfide
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arsenate detoxification III (mycothiol)
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SYSTEMATIC NAME
IUBMB Comments
arseno-mycothiol:mycoredoxin oxidoreductase
Reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by EC 2.8.4.2 (arsenate:mycothiol transferase). A second mycothiol recycles mycoredoxin and forms mycothione.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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heterologous expression of Strop1447 is not able to rescue a yeast strain lacking arsenate reductase acr2
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arseno-mycothiol + mycoredoxin
arsenite + mycothiol-mycoredoxin disulfide
show the reaction diagram
insulin + dithiothreitol
?
show the reaction diagram
D9Q987
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arseno-mycothiol + mycoredoxin
arsenite + mycothiol-mycoredoxin disulfide
show the reaction diagram
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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
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
mycothiol
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
D9Q987
the enzyme activity is reduced by 80% in the presence of CoA
Diamide
D9Q987
the enzyme activity is reduced by 95% in the presence of diamide
ergothioneine
D9Q987
the enzyme activity is reduced by 10% in the presence of ergothioneine
GSH
D9Q987
the enzyme activity is reduced by 60% in the presence of GSH
heparin
D9Q987
the enzyme activity is reduced by about 92% in the presence of heparin
hesperetin
D9Q987
the enzyme activity is reduced by about 75% in the presence of hesperitin
hesperidin
D9Q987
the enzyme activity is reduced by about 87% in the presence of hesperidin
suramin
D9Q987
the enzyme activity is reduced by about 87% in the presence of suramin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
D9Q987
more than 60% activity between pH 7.0 and 8.0
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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Western blot
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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isoform mycoredoxin-1 gets S-mycothiolated on its N-terminal nucleophilic cysteine residue
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solution structures of oxidized and reduced mycoredoxin-1 reveal a thioredoxin fold with a putative mycothiol-binding site
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 75 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and yeast
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C22S
the mutant displays a slightly higher reducing activity toward mixed disulfides compared to the wild type enzyme
C22S
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the mutant displays a slightly higher reducing activity toward mixed disulfides compared to the wild type enzyme
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