Information on EC 1.8.1.6 - cystine reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.8.1.6
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RECOMMENDED NAME
GeneOntology No.
cystine reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-cysteine + NAD+ = L-cystine + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cysteine metabolism
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Cysteine and methionine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-18-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the member of the thioredoxin (Trx)-fold protein family. The enzyme lacks activity with classical thioredoxin, Trx1, substrates. Human enzyme TRP14 has high enzymatic activity in reduction of L-cystine, where the catalytic efficiency coupled to Trx reductase 1 (TrxR1) using NADPH is fivefold higher than the activity of enzyme Trx1 alone. Trx1-mediated L-cystine reduction is inefficient in the presence of other preferred Trx1 substrates whereas, conversely, TRP14 seems to be a more dedicated L-cystine reductase
additional information
the disulfide/dithiol motif formed by Cys43 and Cys46 is the active site of TRP14
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cystine + glutathione
L-cysteine + GSSG
show the reaction diagram
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?
L-cystine + NADH + H+
2 L-cysteine + NAD+
show the reaction diagram
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?
NADH + L-cystine
?
show the reaction diagram
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the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
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NADH + L-cystine
NAD+ + L-cysteine
show the reaction diagram
NADH + L-cystine + H+
NAD+ + L-cysteine
show the reaction diagram
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
L-cystine + NADH + H+
2 L-cysteine + NAD+
show the reaction diagram
Q9BRA2
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?
NADH + L-cystine
?
show the reaction diagram
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the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
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additional information
?
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Q9BRA2
enzyme TRP14 not being able to reduce any classical protein disulfide substrates of thioredoxin 1, Trx1. Trx1-mediated L-cystine reduction is inefficient in the presence of other preferred Trx1 substrates whereas, conversely, TRP14 seems to be a more dedicated L-cystine reductase
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amphotericin
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100% inhibition at a concentration of 0.032 mg/ml
chlorpromazine
ketoconazole
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100% inhibition at a concentration of 0.032 mg/ml
Mepacrine
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100% inhibition at a concentration of 0.032 mg/ml
metronidazole
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26% inhibition at a concentration of 0.032 mg/ml
miconazole
p-Chloromercuriphenylsulfonic acid
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strong
Pentamidine
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58% inhibition at a concentration of 0.032 mg/ml
trifluoroperazine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amphotericin
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29% enhancement of activity at a concentration of 0.032 mg/ml
Mepacrine
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56% enhancement of activity at a concentration of 0.032 mg/ml
metronidazole
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4fold stimulation at a concentration of 0.032 mg/ml
rifampicin
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147% enhancement of activity at a concentration of 0.032 mg/ml
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.9
L-cystine
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30.3
L-cystine
pH 7.5, 22°C, wild-type enzyme TRP14
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
37875
L-cystine
pH 7.5, 22°C, wild-type enzyme TRP14
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high enzyme expression level
Manually annotated by BRENDA team
additional information
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the enzyme is phase specific it is not present in mycelium appears early in the transition of mycelium to yeast
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography
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recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C43S/C46S
site-directed mutagenesis, inactive mutant
C46S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
knockdown and overexpression of TRP14 affect total L-cystine reduction capacity and S-nitrosoprotein levels in crude HEK-293 cell lysate