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Literature summary for 1.21.4.2 extracted from

  • Dietrichs, D.; Meyer, M.; Rieth, M.; Andreesen, J.R.
    Interaction of selenoprotein PA and the thioredoxin system, components of the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and Clostridium litorale. [Erratum to document cited in CA116(1):2789b] (1992), J. Bacteriol., 173, 5983-5991.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
additional information antibodies raised against the thioredoxin reductase-like flavoprotein or thioredoxin inhibit to a high extent Peptoclostridium acidaminophilum

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Peptoclostridium acidaminophilum
-
-
-
Peptoclostridium litorale
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein selenoprotein A is a glycoprotein Peptoclostridium acidaminophilum
glycoprotein selenoprotein A is a glycoprotein Peptoclostridium litorale

Purification (Commentary)

Purification (Comment) Organism
of selenoprotein component PA by 75Se incorporation Peptoclostridium acidaminophilum
of selenoprotein component PA by 75Se incorporation Peptoclostridium litorale

Reaction

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
a
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
a
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
a

Renatured (Commentary)

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 and Products (Substrate)

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

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