Serine dehydratase

Serine dehydratase
Identifiers
SymbolSDS
NCBI gene10993
HGNC10691
OMIM182128
RefSeqNM_006843
UniProtP20132
Other data
EC number4.3.1.17
LocusChr. 12 q24.21
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StructuresSwiss-model
DomainsInterPro

Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structure and properties vary among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. SDH catalyzes the deamination of L-serine to yield pyruvate, with the release of ammonia.[1]

This enzyme has one substrate, L-serine, and two products, pyruvate and NH3, and uses one cofactor, pyridoxal phosphate (PLP). The enzyme's main role is in gluconeogenesis in the liver's cytoplasm.[citation needed]

  1. ^ Sun L, Bartlam M, Liu Y, Pang H, Rao Z (March 2005). "Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver". Protein Science. 14 (3): 791–8. doi:10.1110/ps.041179105. PMC 2279282. PMID 15689518.