The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
L-serine = pyruvate + NH3 (overall reaction) (1a) L-serine = 2-aminoprop-2-enoate + H2O (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous) (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. In humans, this enzymatic activity is found in the proteins encoded by the genes SDS, SDSL, and potentially SRR. The systematic name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1P5J, PDB: 1PWE, PDB: 1PWH, and PDB: 2IQQ.
References
Ramos F, Wiame JM (1982). "Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae". Eur. J. Biochem. 123 (3): 571–6. doi:10.1111/j.1432-1033.1982.tb06570.x. PMID 7042346. Simon D, Hoshino J, Kroger H (1973). "L-serine dehydratase from rat liver. Purification and some properties". Biochim. Biophys. Acta. 321 (1): 361–8. doi:10.1016/0005-2744(73)90091-0. PMID 4750769. Suda M, Nakagawa H (1971). "L-serine dehydratase (Rat liver)". Metabolism of Amino Acids and Amines Part B. Methods Enzymol. Vol. 17B. pp. 346–351. doi:10.1016/0076-6879(71)17060-7. ISBN 978-0-12-181877-7. Sagers RD, Carter JE (1971). "L-serine dehydratase (Clostridium acidiurici)". Metabolism of Amino Acids and Amines Part B. Methods Enzymol. Vol. 17B. pp. 351–356. doi:10.1016/0076-6879(71)17061-9. ISBN 978-0-12-181877-7. Robinson WG, Labow R (1971). "D-serine dehydrase (Escherichia coli)". Metabolism of Amino Acids and Amines Part B. Methods Enzymol. Vol. 17B. pp. 356–360. doi:10.1016/0076-6879(71)17062-0. ISBN 978-0-12-181877-7.


