Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | antibodies raised against the thioredoxin reductase-like flavoprotein or thioredoxin inhibit to a high extent | Peptoclostridium acidaminophilum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
18500 | - |
selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences | Peptoclostridium acidaminophilum |
18500 | - |
selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences | Peptoclostridium litorale |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl phosphate + NH3 + thioredoxin disulfide + H2O | Peptoclostridium acidaminophilum | - |
glycine + phosphate + thioredoxin | - |
? | |
acetyl phosphate + NH3 + thioredoxin disulfide + H2O | Peptoclostridium litorale | - |
glycine + phosphate + thioredoxin | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Peptoclostridium acidaminophilum | - |
- |
- |
Peptoclostridium litorale | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | selenoprotein A is a glycoprotein | Peptoclostridium acidaminophilum |
glycoprotein | selenoprotein A is a glycoprotein | Peptoclostridium litorale |
Purification (Comment) | Organism |
---|---|
of selenoprotein component PA by 75Se incorporation | Peptoclostridium acidaminophilum |
of selenoprotein component PA by 75Se incorporation | Peptoclostridium litorale |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin | the thioredoxin system is involved in the electron transport from reduced pyridine nucleotides to protein A, i.e. in the electron flow between protein of glycine decarboxylase and glycine reductase complex | Peptoclostridium acidaminophilum | |
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin | The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase) | Peptoclostridium acidaminophilum | |
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin | The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase) | Peptoclostridium litorale |
Renatured (Comment) | Organism |
---|---|
denaturation with SDS and 2-mercaptoethanol for 15 min at 100°C does not lead to degradation of protein PA | Peptoclostridium acidaminophilum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl phosphate + NH3 + thioredoxin disulfide + H2O | - |
Peptoclostridium acidaminophilum | glycine + phosphate + thioredoxin | - |
? | |
acetyl phosphate + NH3 + thioredoxin disulfide + H2O | - |
Peptoclostridium litorale | glycine + phosphate + thioredoxin | - |
? | |
acetyl phosphate + NH3 + thioredoxin disulfide + H2O | enzyme activity is NADPH-dependent but not dithioerythritol-dependent | Peptoclostridium acidaminophilum | glycine + phosphate + thioredoxin | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences | Peptoclostridium acidaminophilum |
monomer | selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences | Peptoclostridium litorale |