Serine dehydratase | |||||||
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Identifiers | |||||||
Symbol | SDS | ||||||
NCBI gene | 10993 | ||||||
HGNC | 10691 | ||||||
OMIM | 182128 | ||||||
RefSeq | NM_006843 | ||||||
UniProt | P20132 | ||||||
Other data | |||||||
EC number | 4.3.1.17 | ||||||
Locus | Chr. 12 q24.21 | ||||||
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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]