EC 1.21.4.2 - Glycine reductase

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IntEnz Enzyme Nomenclature
EC 1.21.4.2

Names

Accepted name:
glycine reductase
Systematic name:
acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase (glycine-forming)

Reaction

Comments:

The reaction is observed only in the direction of glycine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Subunit 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 subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0030699
UniProtKB/Swiss-Prot: (22) [show] [UniProt]

References

  1. Wagner, M., Sonntag, D., Grimm, R., Pich, A. Eckerskorn, C., Söhling, B. and Andreesen, J.R.
    Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum.
    Eur. J. Biochem. 260: 38-49 (1999). [PMID: 10091582]
  2. Bednarski, B., Andreesen, J.R. and Pich, A.
    In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue.
    Eur. J. Biochem. 268: 3538-3544 (2001). [PMID: 11422384]

[EC 1.21.4.2 created 2003]