EC 4.3.1.18 - D-serine ammonia-lyase

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IntEnz Enzyme Nomenclature
EC 4.3.1.18

Names

Accepted name:
D-serine ammonia-lyase
Other names:
D-hydroxy amino acid dehydratase
D-hydroxyaminoacid dehydratase
D-serine deaminase
D-serine dehydrase
D-serine dehydratase (deaminating)
D-serine hydro-lyase (deaminating)
D-serine hydrolase
D-serine dehydratase
Systematic name:
D-serine ammonia-lyase (pyruvate-forming)

Reactions

Cofactor

Comments:

A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14, D-serine dehydratase) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008721
CAS Registry Number: 9015-88-7
UniProtKB/Swiss-Prot: (119) [show] [UniProt]

References

  1. Dupourque, D., Newton, W.A. and Snell, E.E.
    Purification and properties of D-serine dehydrase from Escherichia coli.
    J. Biol. Chem. 241: 1233-1238 (1966). [PMID: 5327100]
  2. Metzler, D.E. and Snell, E.E.
    Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme from Escherichia coli.
    J. Biol. Chem. 198: 363-373 (1952). [PMID: 12999751]

[EC 4.3.1.18 created 1961 as EC 4.2.1.14, transfered 2001 to EC 4.3.1.18]