The Enzyme Database

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Accepted name: D-serine ammonia-lyase
Reaction: D-serine = pyruvate + NH3 (overall reaction)
(1a) D-serine = 2-aminoprop-2-enoate + H2O
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
Other name(s): D-hydroxyaminoacid dehydratase; D-serine dehydrase; D-hydroxy amino acid dehydratase; D-serine hydrolase; D-serine dehydratase (deaminating); D-serine deaminase; D-serine hydro-lyase (deaminating)
Systematic name: D-serine ammonia-lyase (pyruvate-forming)
Comments: A pyridoxal-phosphate protein. The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme’s original classification as EC, 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, 2-iminobutanoate/2-iminopropanoate deaminase. Also acts, slowly, on D-threonine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9015-88-7
1.  Dupourque, D., Newton, W.A. and Snell, E.E. Purification and properties of D-serine dehydrase from Escherichia coli. J. Biol. Chem. 241 (1966) 1233–1238. [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 (1952) 363–373. [PMID: 12999751]
[EC created 1961 as EC, transferred 2001 to EC]

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