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Information on EC 1.8.1.6 - cystine reductase
for references in articles please use BRENDA:EC1.8.1.6
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.1 With NAD+ or NADP+ as acceptor
1.8.1.6 cystine reductase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.8.1.6
-
thioredoxin-related
- myoglobin
- trx1
- whale
- apomyoglobins
-
trx-related
-
1.11.1.9
showSynonyms
trp14, cyddc, txndc17, cystine reductase, thioredoxin domain containing 17, txnl5, l-cystine reductase, nadh-dependent cystine reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CysR
cystine reductase (NADH)
-
-
-
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cystine reductase (NADH2)
-
-
-
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EC 1.6.4.1
-
-
formerly
-
L-cysteine:NAD+ oxidoreductase
-
-
-
-
NADH-dependent cystine reductase
-
-
-
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NADH2:L-cystine oxidoreductase
-
-
-
-
reductase, cystine
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 L-cysteine + NAD+ = L-cystine + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
reduction
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-
-
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reduction
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the C-terminal portion of the 5'-adenylyl sulfate reductase from Enteromorpha intestinalis exhibits the cystine reductase activity characteristic of glutaredoxins
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SYSTEMATIC NAME
IUBMB Comments
L-cysteine:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9029-18-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + L-cystine
?
-
Substrates: the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
Products: -
Products: -
?
NADH + L-cystine
NAD+ + L-cysteine
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Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TRP14 has S-denitrosylase activity performing GSNO reduction with realease of NO, it is also active with L-CysSNO
Products: -
Products: -
?
additional information
?
-
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Substrates: enzyme TRP14 has S-denitrosylase activity performing GSNO reduction with realease of NO, it is also active with L-CysSNO
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + L-cystine
?
-
Substrates: the enzyme may provide reduced sulfhydryl groups involved in the transition of mycelium to yeast form
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amphotericin
-
29% enhancement of activity at a concentration of 0.032 mg/ml
Mepacrine
-
56% enhancement of activity at a concentration of 0.032 mg/ml
rifampicin
-
147% enhancement of activity at a concentration of 0.032 mg/ml
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colorectal Neoplasms
Retraction notice to "STAT3-dependent TXNDC17 expression mediates Taxol resistance through inducing autophagy in human colorectal cancer cells" [GENE 584 (1) (2016) 75-82].
Colorectal Neoplasms
STAT3-dependent TXNDC17 expression mediates Taxol resistance through inducing autophagy in human colorectal cancer cells.
Decompression Sickness
Dynorphin-phospholipid membrane interactions: role of phospholipid head-group and cholesterol.
Hypersensitivity
CydDC functions as a cytoplasmic cystine reductase to sensitize Escherichia coli to oxidative stress and aminoglycosides.
Hypersensitivity
Isogenic mutations in the Moraxella catarrhalis CydDC system display pleiotropic phenotypes and reveal the role of a palindrome sequence in its transcriptional regulation.
Infections
The CydDC Family of Transporters and Their Roles in Oxidase Assembly and Homeostasis.
Neoplasms
Dynein light chain LC8 negatively regulates NF-kappaB through the redox-dependent interaction with IkappaBalpha.
Neoplasms
Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways.
Neoplasms
Suberoylanilide hydroxamic acid sensitizes neuroblastoma to paclitaxel by inhibiting thioredoxin-related protein 14-mediated autophagy.
Neoplasms
Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: Implication in the redox regulation of TNF-alpha signaling.
Neuroblastoma
Suberoylanilide hydroxamic acid sensitizes neuroblastoma to paclitaxel by inhibiting thioredoxin-related protein 14-mediated autophagy.
Ovarian Neoplasms
TRP14 promotes resistance to cisplatin by inducing autophagy in ovarian cancer.
Ovarian Neoplasms
TXNDC17 promotes paclitaxel resistance via inducing autophagy in ovarian cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the enzyme is phase specific it is not present in mycelium appears early in the transition of mycelium to yeast
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
metabolism
-
the enzyme complex CydDC does not export L-cysteine from cytoplasm, but rather reduces cytoplasmic cystine
physiological function
-
the enzyme sensitizes Escherichia coli to oxidative (H2O2) stress and aminoglycosides
additional information
additional information
the disulfide/dithiol motif formed by Cys43 and Cys46 is the active site of TRP14
additional information
-
the disulfide/dithiol motif formed by Cys43 and Cys46 is the active site of TRP14
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q7P0N6_CHRVO
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
163
0
17477
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C46S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
additional information
knockdown and overexpression of TRP14 affect total L-cystine reduction capacity and S-nitrosoprotein levels in crude HEK-293 cell lysate
additional information
-
knockdown and overexpression of TRP14 affect total L-cystine reduction capacity and S-nitrosoprotein levels in crude HEK-293 cell lysate
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Romano, A.H.; Nickerson, W.J.
Cystine reductase of pea seeds and yeasts
J. Biol. Chem.
208
409-416
1954
Candida albicans, Pisum sativum, Saccharomyces cerevisiae
brenda
Maresca, B.; Jacobson, E.; Medoff, G.; Kobayashi, G.
Cystine reductase in the dimorphic fungus Histoplasma capsulatum
J. Bacteriol.
135
987-992
1978
Histoplasma capsulatum
brenda
Thibert, R.J.; Sarwar, M.; Carroll, J.E.
Simultaneous determination of cysteine and cystine using N-bromosuccinimide: application in an enzymic system - cystine reductase
Mikrochim. Acta
3
615-624
1969
Saccharomyces cerevisiae
-
brenda
Carroll, J.E.; Kosicki, G.W.; Thibert, R.J.
alpha-Substituted cystines as possible substrates for cystine reductase and L-amino acid oxidase
Biochim. Biophys. Acta
198
601-603
1970
Saccharomyces cerevisiae
brenda
Kim, S.K.; Rahman, A.; Conover, R.C.; Johnson, M.K.; Mason, J.T.; Gomes, V.; Hirasawa, M.; Moore, M.L.; Leustek, T.; Knaff, D.B.
Properties of the cysteine residues and the iron-sulfur cluster of the assimilatory 5-adenylyl sulfate reductase from Enteromorpha intestinalis
Biochemistry
45
5010-5018
2006
Ulva intestinalis
brenda
Ondarza, R.N.; Iturbe, A.; Hernandez, E.
The effects by neuroleptics, antimycotics and antibiotics on disulfide reducing enzymes from the human pathogens Acanthamoeba polyphaga and Naegleria fowleri
Exp. Parasitol.
115
41-47
2007
Acanthamoeba polyphaga, Naegleria fowleri
brenda
Pader, I.; Sengupta, R.; Cebula, M.; Xu, J.; Lundberg, J.O.; Holmgren, A.; Johansson, K.; Arner, E.S.
Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase
Proc. Natl. Acad. Sci. USA
111
6964-6969
2014
Homo sapiens (Q9BRA2), Homo sapiens
brenda
Mironov, A.; Seregina, T.; Shatalin, K.; Nagornykh, M.; Shakulov, R.; Nudler, E.
CydDC functions as a cytoplasmic cystine reductase to sensitize Escherichia coli to oxidative stress and aminoglycosides
Proc. Natl. Acad. Sci. USA
117
23565-23570
2020
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 1.8.1.6)
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Release 2023.1 (January 2023)
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