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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Hordeum vulgare | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Hordeum vulgare |
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 | 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 | Comment | Organism |
---|---|---|
HvNTR1 | - |
Hordeum vulgare |
HvNTR2 | - |
Hordeum vulgare |
NADPH-dependent thioredoxin reductase | - |
Hordeum vulgare |
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 | Comment | Organism | Structure |
---|---|---|---|
FAD | noncovalently bound to HvNTR | Hordeum vulgare | |
NADPH | - |
Hordeum vulgare |