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Literature summary extracted from

  • 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 (2014), Proc. Natl. Acad. Sci. USA, 111, 6964-6969 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.6 recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.6 C43S/C46S site-directed mutagenesis, inactive mutant Homo sapiens
1.8.1.6 C46S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Homo sapiens
1.8.1.6 additional information knockdown and overexpression of TRP14 affect total L-cystine reduction capacity and S-nitrosoprotein levels in crude HEK-293 cell lysate Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.6 additional information
-
 additional information Michaelis-Menten kinetics Homo sapiens
1.8.1.6 0.0008
-
 L-cystine pH 7.5, 22°C, wild-type enzyme TRP14 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.1.6 cytosol
-
 Homo sapiens 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.6 L-cystine + NADH + H+ Homo sapiens
-
 2 L-cysteine + NAD+
-
 ?
1.8.1.6 additional information Homo sapiens 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.6 Homo sapiens Q9BRA2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.6 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.6 A-431 cell high enzyme expression level Homo sapiens
-
1.8.1.6 HEK-293 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.6 L-cystine + NADH + H+
-
 Homo sapiens 2 L-cysteine + NAD+
-
 ?
1.8.1.6 additional information 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 Homo sapiens ?
-
 ?
1.8.1.6 additional information enzyme TRP14 has S-denitrosylase activity performing GSNO reduction with realease of NO, it is also active with L-CysSNO Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.6 L-cystine reductase
-
 Homo sapiens
1.8.1.6 thioredoxin domain containing 17
-
 Homo sapiens
1.8.1.6 thioredoxin-like 5
-
 Homo sapiens
1.8.1.6 TRP14
-
 Homo sapiens
1.8.1.6 TXNDC17
-
 Homo sapiens
1.8.1.6 TXNL5
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.6 22
-
 assay at room temperature Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.6 30.3
-
 L-cystine pH 7.5, 22°C, wild-type enzyme TRP14 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.6 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.6 NADH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.1.6 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 Homo sapiens
1.8.1.6 additional information the disulfide/dithiol motif formed by Cys43 and Cys46 is the active site of TRP14 Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.1.6 37875
-
 L-cystine pH 7.5, 22°C, wild-type enzyme TRP14 Homo sapiens