2-dehydro-3-deoxy-6-phosphogalactonate aldolase

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2-dehydro-3-deoxy-6-phosphogalactonate aldolase
Identifiers
EC no. 4.1.2.21
CAS no. 9030-99-3
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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PMC articles
PubMed articles
NCBI proteins

The enzyme 2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.21) catalyzes the chemical reaction

2-dehydro-3-deoxy-D-galactonate 6-phosphate pyruvate + D-glyceraldehyde 3-phosphate

This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-dehydro-3-deoxy-D-galactonate-6-phosphate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming). Other names in common use include 6-phospho-2-keto-3-deoxygalactonate aldolase, phospho-2-keto-3-deoxygalactonate aldolase, 2-keto-3-deoxy-6-phosphogalactonic aldolase, phospho-2-keto-3-deoxygalactonic aldolase, 2-keto-3-deoxy-6-phosphogalactonic acid aldolase, (KDPGal)aldolase, 2-dehydro-3-deoxy-D-galactonate-6-phosphate, and D-glyceraldehyde-3-phosphate-lyase. This enzyme participates in galactose metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2V81 and 2V82.

Related Research Articles

<span class="mw-page-title-main">Entner–Doudoroff pathway</span>

The Entner–Doudoroff pathway is a metabolic pathway that is most notable in Gram-negative bacteria, certain Gram-positive bacteria and archaea. Glucose is the substrate in the ED pathway and through a series of enzyme assisted chemical reactions it is catabolized into pyruvate. Entner and Doudoroff (1952) and MacGee and Doudoroff (1954) first reported the ED pathway in the bacterium Pseudomonas saccharophila. While originally thought to be just an alternative to glycolysis (EMP) and the pentose phosphate pathway (PPP), some studies now suggest that the original role of the EMP may have originally been about anabolism and repurposed over time to catabolism, meaning the ED pathway may be the older pathway. Recent studies have also shown the prevalence of the ED pathway may be more widespread than first predicted with evidence supporting the presence of the pathway in cyanobacteria, ferns, algae, mosses, and plants. Specifically, there is direct evidence that Hordeum vulgare uses the Entner–Doudoroff pathway.

The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction

The enzyme 2-dehydro-3-deoxy-D-pentonate aldolase 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 2-dehydro-3-deoxy-L-pentonate aldolase catalyzes the chemical reaction

<span class="mw-page-title-main">2-Dehydro-3-deoxy-phosphogluconate aldolase</span> Class of enzymes

The enzyme 2-dehydro-3-deoxy-phosphogluconate aldolase, commonly known as KDPG aldolase, catalyzes the chemical reaction

The enzyme 3-deoxy-D-manno-octulosonate aldolase catalyzes the chemical reaction

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

The enzyme 5-dehydro-2-deoxyphosphogluconate aldolase catalyzes the chemical reaction

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

The enzyme N-acetylneuraminate lyase catalyzes the chemical reaction

The enzyme 2-dehydro-3-deoxy-L-arabinonate dehydratase (EC 4.2.1.43) catalyzes the chemical reaction

The enzyme D-fuconate dehydratase (EC 4.2.1.67) catalyzes the chemical reaction.

The enzyme galactonate dehydratase (EC 4.2.1.6) catalyzes the chemical reaction

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

The enzyme phosphogluconate dehydratase (EC 4.2.1.12) catalyzes the chemical reaction

In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2-dehydro-3-deoxygalactonokinase is an enzyme that catalyzes the chemical reaction

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

In enzymology, a 2-dehydro-3-deoxygluconokinase is an enzyme that catalyzes the chemical reaction

In enzymology, a 5-dehydro-2-deoxygluconokinase is an enzyme that catalyzes the chemical reaction

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

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.

References


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