General Information:
Id: | 14,377 |
Diseases: |
Metabolic
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Homo sapiens | |
article | |
Reference: | Johansson C et al.(2004) Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase J Biol Chem 279: 7537-7543 [PMID: 14676218] |
Interaction Information:
Comment | Grx2 is a direct substrate for thioredoxin reductase and thus acts as a thioredoxin, being able to accept electrons from both TrxR1 and TrxR2 as well as from GSH. Using this novel electron donor pathway, Grx2 reduced low molecular weight disulfides such as CoA but with particular high efficiency glutathionylated substrates including GSSG. These results suggest an important role for Grx2 in protection and recovery from oxidative stress. |
Formal Description Interaction-ID: 135703 |
gene/protein decreases_activity of process |
Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Since TrxR1 and TrxR2 from various species reveal almost identical kinetic parameters, one can expect human mitochondrial TrxR2 to reduce Grx2 with an efficiency similar to that of the bovine TrxR1. Activity with the monothiol active site mutant Grx2C40S, in a coupled assay with Cys-SG, demonstrated further that TrxR can support both monothiol and dithiol reactions catalyzed by Grx2. This suggests that the glutaredoxin-GSH-mixed disulfide is attacked by the selenolate in TrxR, forming a mixed disulfide intermediate, releasing the glutathione moiety, revealing a new glutathione-independent path of electron flow from NADPH to various Grx substrates. |
Formal Description Interaction-ID: 135704 |
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Drugbank entries | Show/Hide entries for GLRX2 or TXNRD1 |
Comment | Complete Trx and the Grx systems in mammalian cells are present both in the cytosol and the mitochondria. |
Formal Description Interaction-ID: 135705 |
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Comment | Grx2 is a direct substrate for thioredoxin reductase and thus acts as a thioredoxin, being able to accept electrons from both TrxR1 and TrxR2 as well as from GSH. Using this novel electron donor pathway, Grx2 reduced low molecular weight disulfides such as CoA but with particular high efficiency glutathionylated substrates including GSSG. These results suggest an important role for Grx2 in protection and recovery from oxidative stress. |
Formal Description Interaction-ID: 135706 |
gene/protein increases_activity of process |
Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Grx2 is a direct substrate for thioredoxin reductase and thus acts as a thioredoxin, being able to accept electrons from both TrxR1 and TrxR2 as well as from GSH. Using this novel electron donor pathway, Grx2 reduced low molecular weight disulfides such as CoA but with particular high efficiency glutathionylated substrates including GSSG. These results suggest an important role for Grx2 in protection and recovery from oxidative stress. |
Formal Description Interaction-ID: 135707 |
gene/protein increases_activity of process |
Drugbank entries | Show/Hide entries for TXNRD1 |
Comment | Grx2 is a direct substrate for thioredoxin reductase and thus acts as a thioredoxin, being able to accept electrons from both TrxR1 and TrxR2 as well as from GSH. Using this novel electron donor pathway, Grx2 reduced low molecular weight disulfides such as CoA but with particular high efficiency glutathionylated substrates including GSSG. These results suggest an important role for Grx2 in protection and recovery from oxidative stress. |
Formal Description Interaction-ID: 135708 |
gene/protein increases_activity of process |
Comment | The results suggest an important role for Grx2 in protection and recovery from oxidative stress. In fact, Grx2 may be a key regulator of apoptosis via the mitochondrial checkpoint. |
Formal Description Interaction-ID: 135712 |
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Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Complete Trx and the Grx systems in mammalian cells are present both in the cytosol and the mitochondria. |
Formal Description Interaction-ID: 135713 |
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Comment | Complete Trx and the Grx systems in mammalian cells are present both in the cytosol and the mitochondria. |
Formal Description Interaction-ID: 135714 |
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Comment | Complete Trx and the Grx systems in mammalian cells are present both in the cytosol and the mitochondria. |
Formal Description Interaction-ID: 135715 |
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Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135717 |
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Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135718 |
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Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135719 |
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Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135720 |
increases_quantity of gene/protein |
Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135721 |
increases_quantity of gene/protein |
Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135722 |
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Drugbank entries | Show/Hide entries for GLRX2 |
Comment | Grx (Grx2) is due to an alternative splicing mechanism targeted either to the nucleus or to mitochondria. Grx2 has a predicted size of 18 kDa and contains a CSYC active site motif that differs from the Grx consensus CPYC. |
Formal Description Interaction-ID: 135723 |
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Drugbank entries | Show/Hide entries for GLRX2 |
Comment | The thioredoxin system is composed of thioredoxin reductase (TrxR), in mammalian cells a selenocysteine-containing, dimeric nicotinamide nucleotide disulfide oxidoreductase, which reduces thioredoxin (Trx), the major protein disulfide reductase with a large number of functions in mammalian cells. |
Formal Description Interaction-ID: 135724 |
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Drugbank entries | Show/Hide entries for TXNRD1 |
Comment | The thioredoxin system is composed of thioredoxin reductase (TrxR), in mammalian cells a selenocysteine-containing, dimeric nicotinamide nucleotide disulfide oxidoreductase, which reduces thioredoxin (Trx), the major protein disulfide reductase with a large number of functions in mammalian cells. |
Formal Description Interaction-ID: 135725 |
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Comment | The thioredoxin system is composed of thioredoxin reductase (TrxR), in mammalian cells a selenocysteine-containing, dimeric nicotinamide nucleotide disulfide oxidoreductase, which reduces thioredoxin (Trx), the major protein disulfide reductase with a large number of functions in mammalian cells. |
Formal Description Interaction-ID: 135726 |
gene/protein decreases_quantity of drug/chemical compound |
Comment | The thioredoxin system is composed of thioredoxin reductase (TrxR), in mammalian cells a selenocysteine-containing, dimeric nicotinamide nucleotide disulfide oxidoreductase, which reduces thioredoxin (Trx), the major protein disulfide reductase with a large number of functions in mammalian cells. |
Formal Description Interaction-ID: 135727 |
gene/protein decreases_quantity of drug/chemical compound |
Drugbank entries | Show/Hide entries for TXNRD1 |