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Literature summary extracted from

  • Kohlstock, U.M.; Rucknagel, K.P.; Reuter, M.; Schierhorn, A.; Andreesen, J.R.; Sohling, B.
    Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum (2001), Eur. J. Biochem., 268, 6417-6425.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.21.4.2 cloning of two subunits of protein C: grdC1 and grdD1, expression in Escherichia coli Peptoclostridium acidaminophilum

Protein Variants

EC Number Protein Variants Comment Organism
1.21.4.2 C359A grdD of protein component C, mutant enzyme completely inactive, accessible to iodoacetate only under native conditions, suggesting that Cys359 of GrdD is the thiol responsible for the formation of the acetyl thioester during catalysis of arsenate-dependent hydrolysis of acetyl phosphate Peptoclostridium acidaminophilum
1.21.4.2 C98S grdD of protein component C, activity is unchanged, accessible to iodoacetate only after denaturation Peptoclostridium acidaminophilum

Inhibitors

EC Number Inhibitors Comment Organism Structure
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 Peptoclostridium acidaminophilum

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 Peptoclostridium acidaminophilum
-
 glycine + phosphate + thioredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.21.4.2 Peptoclostridium acidaminophilum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.21.4.2 of protein C of enzyme, recombinant enzyme Peptoclostridium acidaminophilum

Reaction

EC Number Reaction Comment Organism Reaction ID
1.21.4.2 acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin GrdD of protein component C catalyses the arsenate-dependent decomposition of acetyl phosphate, whereas GrdC completely inactive Peptoclostridium acidaminophilum
a
1.21.4.2 acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin Cys 359 of GrdD is the thiol responsible for the formation of the acetyl thioester during catalysis of arsenate-dependent hydrolysis of acetyl phosphate Peptoclostridium acidaminophilum
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) Peptoclostridium acidaminophilum
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
-
 Peptoclostridium acidaminophilum glycine + phosphate + thioredoxin
-
 ?