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Literature summary extracted from

  • Stadtman, T.C.; Davis, J.N.
    Glycine reductase protein C. Properties and characterization of its role in the reductive cleavage of Se-carboxymethyl-selenoprotein A (1991), J. Biol. Chem., 266, 22147-22153.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.21.4.2 arsenate absolutely required for protein C activity Acetoanaerobium sticklandii

General Stability

EC Number General Stability Organism
1.21.4.2 the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited by alkylation selenoprotein A alkylated at pH 6 with bromoacetate is active as a component of the enzyme complex Acetoanaerobium sticklandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.21.4.2 (NH4)2SO4 inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate Acetoanaerobium sticklandii
1.21.4.2 Bromoacetate 75Se-labeled protein A preparation is inactivated at pH 6, 25°C, for 10 min in presence of 10 mM bromoacetate by about 25% Acetoanaerobium sticklandii
1.21.4.2 iodoacetate the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited, but protein C is protected from inactivation by treatment acetyl phosphate Acetoanaerobium sticklandii
1.21.4.2 KCl the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited Acetoanaerobium sticklandii

Natural Substrates/ Products (Substrates)

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 Acetoanaerobium sticklandii
-
glycine + phosphate + thioredoxin
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.21.4.2 Acetoanaerobium sticklandii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.21.4.2 of protein C of enzyme Acetoanaerobium sticklandii

Reaction

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 Acetoanaerobium sticklandii
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) Acetoanaerobium sticklandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.21.4.2 acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Acetoanaerobium sticklandii glycine + phosphate + thioredoxin
-
?
1.21.4.2 additional information Se-carboxymethyl selenprotein A is a substrate of protein C Acetoanaerobium sticklandii ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.21.4.2 47
-
30% loss of activity of protein C after heating for 10 min, at pH 7.0, in the presence of EDTA, with and without Mg2+ Acetoanaerobium sticklandii
1.21.4.2 68
-
80% loss of activity of protein C after heating for 10 min, at pH 7.0, in the presence of EDTA, with and without Mg2+ Acetoanaerobium sticklandii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.21.4.2 additional information
-
pI of protein component C: 5.7 Acetoanaerobium sticklandii