Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.21.4.2 extracted from

  • Arkowitz, R.A.; Abeles, R.H.
    Mechanism of action of clostridial glycine reductase: isolation and characterization of a covalent acetyl enzyme intermediate (1991), Biochemistry, 30, 4090-4097.
    View publication on PubMed
Search for more literature for 1.21.4.2

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
-
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin mechanism, thiols are present in protein C that is acetylated during reaction 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
-
 ?