Tartronate-semialdehyde synthase

Last updated
tartronate-semialdehyde synthase
2pan.jpg
Tartronate-semialdehyde synthase homotetramer, E.Coli
Identifiers
EC no. 4.1.1.47
CAS no. 9027-24-1
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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme tartronate-semialdehyde synthase (EC 4.1.1.47) catalyzes the chemical reaction

2 glyoxylate tartronate semialdehyde + CO2

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is glyoxylate carboxy-lyase (dimerizing tartronate-semialdehyde-forming). Other names in common use include tartronate semialdehyde carboxylase, glyoxylate carbo-ligase, glyoxylic carbo-ligase, hydroxymalonic semialdehyde carboxylase, tartronic semialdehyde carboxylase, glyoxalate carboligase, and glyoxylate carboxy-lyase (dimerizing). This enzyme participates in glyoxylate and dicarboxylate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

Related Research Articles

Carboxy-lyases, also known as decarboxylases, are carbon–carbon lyases that add or remove a carboxyl group from organic compounds. These enzymes catalyze the decarboxylation of amino acids, beta-keto acids and alpha-keto acids.

<span class="mw-page-title-main">Phosphoenolpyruvate carboxylase</span> Class of enzymes

Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3−) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate:

<span class="mw-page-title-main">Phosphoribosylaminoimidazole carboxylase</span> Enzyme involved in purine synthesis

The enzyme Phosphoribosylaminoimidazole carboxylase, or AIR carboxylase (EC 4.1.1.21) is involved in nucleotide biosynthesis and in particular in purine biosynthesis. It catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole ("AIR") into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole ("CAIR") as described in the reaction:

In enzymology, a [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase (EC 2.1.1.127) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">2-dehydro-3-deoxyglucarate aldolase</span> Class of enzymes

The enzyme 2-dehydro-3-deoxyglucarate aldolase catalyzes the chemical reaction

The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction

The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction

The enzyme 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase (EC 4.1.1.68) catalyzes the chemical reaction

<span class="mw-page-title-main">Aminocarboxymuconate-semialdehyde decarboxylase</span>

The enzyme aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) catalyzes the chemical reaction

<span class="mw-page-title-main">Aspartate 1-decarboxylase</span>

The enzyme aspartate 1-decarboxylase (EC 4.1.1.11) catalyzes the chemical reaction

The enzyme diaminobutyrate decarboxylase (EC 4.1.1.86) catalyzes the chemical reaction

The enzyme dihydroxyfumarate decarboxylase (EC 4.1.1.54) 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

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

Isocitrate lyase, or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate. Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle and is used by bacteria, fungi, and plants.

<span class="mw-page-title-main">Oxalyl-CoA decarboxylase</span>

The enzyme oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction

The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) catalyzes the chemical reaction

<span class="mw-page-title-main">Phosphoribosylaminoimidazolesuccinocarboxamide synthase</span> Class of enzymes

In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Malate synthase</span> Class of enzymes

In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction

Isocitrate lyase family is a family of evolutionarily related proteins.

<span class="mw-page-title-main">Dihydrodipicolinate synthase</span> Class of enzymes

4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction

References


    This page is based on this Wikipedia article
    Text is available under the CC BY-SA 4.0 license; additional terms may apply.
    Images, videos and audio are available under their respective licenses.