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Literature summary for 1.21.4.2 extracted from

  • Schraeder, T.; Andreesen, J.R.
    Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum (1992), Eur. J. Biochem., 206, 79-85.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
arsenate absolutely required for protein C activity Peptoclostridium acidaminophilum
thiols not absolutely required, but increases activity by about 20%, the highest enzyme activity in presence of 10 mM dithioerythritol Peptoclostridium acidaminophilum

Inhibitors

Inhibitors Comment Organism Structure
(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
acetyl phosphate inhibits protein C activity, although a substrate Peptoclostridium acidaminophilum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ not absolutely required, but increases activity by about 20%, the highest enzyme activity in presence of 10 mM MgCl2 Peptoclostridium acidaminophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE Peptoclostridium acidaminophilum
57000
-
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE Peptoclostridium acidaminophilum
420000
-
protein component C, gel filtration 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
of protein C of enzyme Peptoclostridium acidaminophilum

Reaction

Reaction Comment Organism Reaction ID
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin the protein C component catalyses the arsenate-dependent decomposition of acetyl phosphate Peptoclostridium acidaminophilum
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
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
additional information
-
-
Peptoclostridium acidaminophilum
51.3
-
protein C of enzyme Peptoclostridium acidaminophilum

Storage Stability

Storage Stability Organism
-20°C, no significant loss of activity during storage 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
-
?
additional information Se-carboxymethyl selenprotein A is a substrate of protein C Peptoclostridium acidaminophilum ?
-
?

Subunits

Subunits Comment Organism
octamer protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE Peptoclostridium acidaminophilum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
of the arsenate dependent decomposition of acetyl phosphate Peptoclostridium acidaminophilum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
of the arsenate dependent decomposition of acetyl phosphate, Tris/HCl buffer Peptoclostridium acidaminophilum
10
-
of the arsenate dependent decomposition of acetyl phosphate, piperazin buffer Peptoclostridium acidaminophilum