EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.21.4.2 | arsenate | absolutely required for protein C activity | Peptoclostridium acidaminophilum | |
1.21.4.2 | thiols | not absolutely required, but increases activity by about 20%, the highest enzyme activity in presence of 10 mM dithioerythritol | Peptoclostridium acidaminophilum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.21.4.2 | (NH4)2SO4 | 70% loss of activity at 300 mM; inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate | Peptoclostridium acidaminophilum | |
1.21.4.2 | acetyl phosphate | inhibits protein C activity, although a substrate | Peptoclostridium acidaminophilum |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.21.4.2 | Mg2+ | not absolutely required, but increases activity by about 20%, the highest enzyme activity in presence of 10 mM MgCl2 | Peptoclostridium acidaminophilum |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.21.4.2 | 48000 | - |
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE | Peptoclostridium acidaminophilum |
1.21.4.2 | 57000 | - |
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE | Peptoclostridium acidaminophilum |
1.21.4.2 | 420000 | - |
protein component C, gel filtration | Peptoclostridium acidaminophilum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.21.4.2 | acetyl phosphate + NH3 + thioredoxin disulfide + H2O | Peptoclostridium acidaminophilum | - |
glycine + phosphate + thioredoxin | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.21.4.2 | Peptoclostridium acidaminophilum | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.21.4.2 | of protein C of enzyme | Peptoclostridium acidaminophilum |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.21.4.2 | acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin | the protein C component catalyses the arsenate-dependent decomposition of acetyl phosphate | Peptoclostridium acidaminophilum | |
1.21.4.2 | acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin | the 48000 Da subunit of protein component C catalyses the arsenate-dependent decomposition of actetyl phosphate, a possible role of the 57000 Da subunit of protein component C could be the involvement in the reductive dehydration which leads to the cleavage of the protein A-bound carboxymethyl-selenoether to ketene and oxidized protein A | Peptoclostridium acidaminophilum | |
1.21.4.2 | 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 |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.21.4.2 | additional information | - |
- |
Peptoclostridium acidaminophilum |
1.21.4.2 | 51.3 | - |
protein C of enzyme | Peptoclostridium acidaminophilum |
EC Number | Storage Stability | Organism |
---|---|---|
1.21.4.2 | -20°C, no significant loss of activity during storage | Peptoclostridium acidaminophilum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.21.4.2 | acetyl phosphate + NH3 + thioredoxin disulfide + H2O | - |
Peptoclostridium acidaminophilum | glycine + phosphate + thioredoxin | - |
? | |
1.21.4.2 | additional information | Se-carboxymethyl selenprotein A is a substrate of protein C | Peptoclostridium acidaminophilum | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.21.4.2 | octamer | protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE | Peptoclostridium acidaminophilum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.21.4.2 | 40 | - |
of the arsenate dependent decomposition of acetyl phosphate | Peptoclostridium acidaminophilum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.21.4.2 | 7.5 | - |
of the arsenate dependent decomposition of acetyl phosphate, Tris/HCl buffer | Peptoclostridium acidaminophilum |
1.21.4.2 | 10 | - |
of the arsenate dependent decomposition of acetyl phosphate, piperazin buffer | Peptoclostridium acidaminophilum |