Literature summary 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.

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	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
1.21.4.2	acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin	mechanism, thiols are present in protein C that is acetylated during reaction	Acetoanaerobium sticklandii	a
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	a

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	-	?

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Release 2023.1 (January 2023)