L-serine ammonia-lyase

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L-serine ammonia-lyase
1p5j.jpg
Serine dehydratase monomer, Human
Identifiers
EC no. 4.3.1.17
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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NCBI proteins

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. 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

<span class="mw-page-title-main">Dehydratase</span> Group of lyase enzymes

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.

<span class="mw-page-title-main">Serine dehydratase</span>

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.

<span class="mw-page-title-main">Cystathionine gamma-lyase</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">Threonine ammonia-lyase</span>

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:

<span class="mw-page-title-main">Anthranilate synthase</span>

The enzyme anthranilate synthase catalyzes the chemical reaction

<span class="mw-page-title-main">Indole-3-glycerol-phosphate synthase</span> Class of enzymes

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

<span class="mw-page-title-main">Glucarate dehydratase</span>

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

<span class="mw-page-title-main">4-hydroxy-tetrahydrodipicolinate reductase</span> InterPro Family

In enzymology, a 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) is an enzyme that catalyzes the chemical reaction

References