This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. 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 1P5J, 1PWE, 1PWH, and 2IQQ.
Related Research Articles
Dehydratases are a group of lyase enzymes that form double and triple bonds in a substrate through the removal of water. They can be found in many places including the mitochondria, peroxisome and cytosol. There are more than 150 different dehydratase enzymes that are classified into four groups. Dehydratases can act on hydroxyacyl-CoA with or without cofactors, and some have a metal and non-metal cluster act as their active site.
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.
The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)) breaks down cystathionine into cysteine, 2-oxobutanoate (α-ketobutyrate), and ammonia:
In enzymology, a putrescine oxidase (EC 1.4.3.10) is an enzyme that catalyzes the chemical reaction
The enzyme 3-chloro-D-alanine dehydrochlorinase (EC 4.5.1.2) catalyzes the reaction
The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction
The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction
The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction
The enzyme homocysteine desulfhydrase (EC 4.4.1.2) catalyzes the chemical reaction
The enzyme L-cysteate sulfo-lyase (EC 4.4.1.25) catalyzes the reaction
The enzyme Serine-sulfate ammonia-lyase (EC 4.3.1.10) catalyzes the chemical reaction
Threonine ammonia-lyase (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L-threonine into α-ketobutyrate and ammonia:
The enzyme anthranilate synthase catalyzes the chemical reaction
The enzyme indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) catalyzes the chemical reaction
The enzyme galactarate dehydratase (EC 4.2.1.42) catalyzes the chemical reaction
The enzyme glucarate dehydratase (EC 4.2.1.40) catalyzes the chemical reaction
In enzymology, a formimidoylglutamate deiminase (EC 3.5.3.13) is an enzyme that catalyzes the chemical reaction
In enzymology, an O-acetylhomoserine aminocarboxypropyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) is an enzyme that catalyzes the chemical reaction
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. PMID4750769.
Suda M, Nakagawa H (1971). L-Serine dehydratase (rat liver). Methods Enzymol. Vol.17B. pp.346–351. doi:10.1016/0076-6879(71)17060-7.
Sagers RD, Carter JE (1971). L-Serine dehydratase (Clostridium acidiurica). Methods Enzymol. Vol.17B. pp.351–356. doi:10.1016/0076-6879(71)17061-9.
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