ExplorEnz: EC 4.3.1.18

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4.3.1.18

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 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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9015-88-7

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 (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 4.3.1.18 created 1961 as EC 4.2.1.14, transferred 2001 to EC 4.3.1.18]