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Literature summary for 1.21.4.2 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
Search for more literature for 1.21.4.2

Activating Compound

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

General Stability

General Stability Organism
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

Inhibitors Comment Organism Structure
(NH4)2SO4 inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate Acetoanaerobium sticklandii
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
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
KCl the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited Acetoanaerobium sticklandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl phosphate + NH3 + thioredoxin disulfide + H2O Acetoanaerobium sticklandii
-
 glycine + phosphate + thioredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Acetoanaerobium sticklandii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
of protein C of enzyme Acetoanaerobium sticklandii

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 Acetoanaerobium sticklandii
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) Acetoanaerobium sticklandii
a

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
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

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