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Literature summary for 1.8.1.9 extracted from

  • Shahpiri, A.; Svensson, B.; Finnie, C.
    The NADPH-dependent thioredoxin reductase/thioredoxin system in germinating barley seeds: gene expression, protein profiles, and interactions between isoforms of thioredoxin h and thioredoxin reductase (2008), Plant Physiol., 146, 789-799.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.9

Cloned(Commentary)

Cloned (Comment) Organism
recombinant protein carrying an amino terminal His6-tag is produced in Escherichia coli Hordeum vulgare
recombinant protein carrying an aminoterminal His6-tag is produced in Escherichia coli Hordeum vulgare

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0009
-
 Hordeum vulgare thioredoxin disulfide h2 pH 5.7, HvNTR2 Hordeum vulgare
0.00112
-
 Hordeum vulgare thioredoxin disulfide h1 pH 7.4, HvNTR2 Hordeum vulgare
0.00118
-
 Hordeum vulgare thioredoxin disulfide h1 pH 7.4, HvNTR1 Hordeum vulgare
0.00129
-
 Hordeum vulgare thioredoxin disulfide h2 pH 7.4, HvNTR2 Hordeum vulgare
0.00145
-
 Hordeum vulgare thioredoxin disulfide h2 pH 5.7, HvNTR1 Hordeum vulgare
0.00179
-
 Hordeum vulgare thioredoxin disulfide h2 pH 7.4, HvNTR1 Hordeum vulgare

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Hordeum vulgare

Source Tissue

Source Tissue Comment Organism Textmining
seed although mRNA encoding both Trx h isoforms (HvTrxh1 and HvTrxh2) is present in embryo and aleurone layers, the corresponding proteins differ in spatiotemporal appearance. HvNTR1 resides in the starchy endosperm during germination Hordeum vulgare
-
seed although mRNA encoding both Trx h isoforms (HvTrxh1 and HvTrxh2) is present in embryo and aleurone layers, the corresponding proteins differ in spatiotemporal appearance. HvNTR2 resides in the starchy endosperm during germination Hordeum vulgare
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+
-
 Hordeum vulgare 2-nitro-5-thiobenzoate + NADP+
-
 ?
Hordeum vulgare thioredoxin disulfide h1 + NADPH + H+
-
 Hordeum vulgare Hordeum vulgare thioredoxin h1 + NADP+
-
 r
Hordeum vulgare thioredoxin disulfide h2 + NADPH + H+
-
 Hordeum vulgare Hordeum vulgare thioredoxin h2 + NADP+
-
 r
thioredoxin disulfide + NADPH + H+ recombinant HvNTR1 and HvNTR2 exhibit virtually the same affinity toward HvTrxh1 and HvTrxh2, whereas HvNTR2 has slightly higher catalytic activity than HvNTR1 with both Trx h isoforms, and HvNTR1 has slightly higher catalytic activity toward HvTrxh1 than HvTrxh2 Hordeum vulgare thioredoxin + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
HvNTR1
-
 Hordeum vulgare
HvNTR2
-
 Hordeum vulgare
NADPH-dependent thioredoxin reductase
-
 Hordeum vulgare

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.43
-
 Hordeum vulgare thioredoxin disulfide h2 pH 5.7, HvNTR1 Hordeum vulgare
0.8
-
 Hordeum vulgare thioredoxin disulfide h2 pH 5.7, HvNTR2 Hordeum vulgare
1.31
-
 Hordeum vulgare thioredoxin disulfide h2 pH 7.4, HvNTR1 Hordeum vulgare
2.25
-
 Hordeum vulgare thioredoxin disulfide h1 pH 7.4, HvNTR1 Hordeum vulgare
2.98
-
 Hordeum vulgare thioredoxin disulfide h2 pH 7.4, HvNTR2 Hordeum vulgare
3.26
-
 Hordeum vulgare thioredoxin disulfide h1 pH 7.4, HvNTR2 Hordeum vulgare

Cofactor

Cofactor Comment Organism Structure
FAD noncovalently bound to HvNTR Hordeum vulgare
NADPH
-
 Hordeum vulgare