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Literature summary for 1.21.4.2 extracted from

  • Wagner, M.; Sonntag, D.; Grimm, R.; Pich, A.; Eckerskorn, C.; Söhling, B.; Andreesen, J.R.
    Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum (1999), Eur. J. Biochem., 260, 38-49.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloning and sequencing of a new gene region, encoding a proprotein for the beta and alpha subunits of selenoprotein B: grdE, selenoprotein A: grdA and selenium-containing gamma subunit of selenoprotein B: grdB Peptoclostridium acidaminophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000 Peptoclostridium acidaminophilum
25000
-
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000 Peptoclostridium acidaminophilum
47000
-
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000 Peptoclostridium acidaminophilum

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
-
?

Organism

Organism UniProt Comment Textmining
Peptoclostridium acidaminophilum Q9R4G7 DSM 5388T, growth on serine
-

Purification (Commentary)

Purification (Comment) Organism
of selenoprotein B of enzyme Peptoclostridium acidaminophilum

Reaction

Reaction Comment Organism Reaction ID
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin mechanism Peptoclostridium acidaminophilum
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin cleavage mechanism for the pyruvoyl group dependent reductase starting from cysteine 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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
352
-
substrate-specific selenoprotein B of enzyme 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
-
?

Subunits

Subunits Comment Organism
hexamer selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000 Peptoclostridium acidaminophilum