Target type: molecularfunction
Catalysis of the reaction: 2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate. [EC:4.1.2.14]
2-dehydro-3-deoxy-phosphogluconate aldolase activity is a crucial step in the pentose phosphate pathway, a vital metabolic pathway that generates NADPH and pentose sugars. This enzyme catalyzes the reversible cleavage of 2-dehydro-3-deoxy-phosphogluconate (KDPG) into pyruvate and glyceraldehyde 3-phosphate. The active site of the enzyme typically utilizes a Schiff base intermediate formed between the substrate and a lysine residue, which facilitates the breakage of the carbon-carbon bond in KDPG. This cleavage reaction is highly specific, with the enzyme exhibiting a strong preference for KDPG over other similar substrates. The aldolase reaction proceeds through a series of steps, including: 1) substrate binding, 2) Schiff base formation, 3) carbon-carbon bond cleavage, 4) release of products, and 5) regeneration of the enzyme. 2-dehydro-3-deoxy-phosphogluconate aldolase activity is essential for various metabolic processes, including nucleotide biosynthesis, fatty acid synthesis, and detoxification reactions. Mutations or deficiencies in this enzyme can lead to metabolic disorders. '
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Protein | Definition | Taxonomy |
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KHG/KDPG aldolase | A KHG/KDPG aldolase that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P0A955] | Escherichia coli K-12 |
Compound | Definition | Classes | Roles |
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2-keto-3-deoxy-6-phosphogluconate | 2-dehydro-3-deoxy-6-phospho-D-gluconic acid : The 5-phospho derivative of 2-dehydro-D-gluconic acid. 2-keto-3-deoxy-6-phosphogluconate: structure given in first source; an intermediate in glucose metabolism | ketoaldonic acid phosphate | Escherichia coli metabolite |