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Results 1 - 6 of 6
EC Number Natural Substrates Commentary (Nat. Sub.)
Show all pathways known for 4.1.3.17Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.174-carboxy-4-hydroxy-2-oxoadipate -
Show all pathways known for 4.1.3.17Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.174-hydroxy-4-methyl-2-oxoglutarate involved in biosynthesis of gamma-substituted glutamic acid, participates in the alpha-keto acid pathway for degradation of the meta-fission product of protocatechuate, in Pseudomonas ochraceae grown on phthalate the physiolological substrate is not hydroxymethyl glutamic acid but CHA, L-4-carboxy-4-hydroxy-2-oxoadipate, which is cleaved to pyruvate and oxaloacetate
Show all pathways known for 4.1.3.17Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.174-hydroxy-4-methyl-2-oxoglutarate -
Show all pathways known for 4.1.3.17Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.17l-4-carboxy-4-hydroxy-2-oxoadipate -
Show all pathways known for 4.1.3.17Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.17more inducible by aromatic carboxylates such as phthalate
Show all pathways known for 4.1.3.17Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.17more the enzyme is a class II, divalent metal ion-dependent, pyruvate aldolase that catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate into two molecules of pyruvate in the former and a molecule of each pyruvate and oxaloacetate in the latter, cf. 4-carboxy-4-hydroxy-2-oxoadipate aldolase, EC 4.1.3. The enzyme also contains a secondary oxaloacetate decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retroaldol and decarboxylase reactions
Results 1 - 6 of 6