Catechol 2,3-dioxygenase (EC 1.13.11.2, 2,3-pyrocatechase, catechol 2,3-oxygenase, catechol oxygenase, metapyrocatechase, pyrocatechol 2,3-dioxygenase) is an enzyme with systematic name catechol:oxygen 2,3-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction
In enzymology, a 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase (EC 1.2.1.60) is an enzyme that catalyzes the chemical reaction
In enzymology, an aminomuconate-semialdehyde dehydrogenase (EC 1.2.1.32) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) is an enzyme that catalyzes the chemical reaction
The enzyme L-2-amino-4-chloropent-4-enoate dehydrochlorinase (EC 4.5.1.4) catalyzes the reaction
In enzymology, a 2,6-dioxo-6-phenylhexa-3-enoate hydrolase (EC 3.7.1.8) is an enzyme that catalyzes the chemical reaction
The enzyme 4-oxalocrotonate decarboxylase (EC 4.1.1.77) catalyzes the chemical reaction
The enzyme 2-oxopent-4-enoate hydratase (EC 4.2.1.80) catalyzes the chemical reaction
In enzymology, a 2-(acetamidomethylene)succinate hydrolase (EC 3.5.1.29) is an enzyme that catalyzes the chemical reaction
In enzymology, 2-aminomuconate deaminase (EC 3.5.99.5) (also known as amnd) is an enzyme that catalyzes the chemical reaction
In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction
In enzymology, an arylformamidase (EC 3.5.1.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-substituted formamide deformylase (EC 3.5.1.91) is an enzyme that catalyzes the chemical reaction
Alpha-aminoadipic semialdehyde synthase is an enzyme encoded by the AASS gene in humans and is involved in their major lysine degradation pathway. It is similar to the separate enzymes coded for by the LYS1 and LYS9 genes in yeast, and related to, although not similar in structure, the bifunctional enzyme found in plants. In humans, mutations in the AASS gene, and the corresponding alpha-aminoadipic semialdehyde synthase enzyme are associated with familial hyperlysinemia. This condition is inherited in an autosomal recessive pattern and is not considered a particularly negative condition, thus making it a rare disease.
2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase (EC 1.1.1.312, 2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase, 4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+ oxidoreductase, alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase, 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase, LigC, ProD) is an enzyme with systematic name 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase. This enzyme catalyses the following chemical reaction
2-Hydroxymuconate-6-semialdehyde dehydrogenase (EC 1.2.1.85, xylG [gene], praB [gene] ) is an enzyme with systematic name (2E,4Z)-2-hydroxy-6-oxohexa-2,4-dienoate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction
Benzoyl-CoA-dihydrodiol lyase (EC 4.1.2.44, 2,3-dihydro-2,3-dihydroxybenzoyl-CoA lyase/hydrolase (deformylating), BoxC, dihydrodiol transforming enzyme, benzoyl-CoA oxidation component C) is an enzyme with systematic name 2,3-dihydro-2,3-dihydroxybenzoyl-CoA 3,4-didehydroadipyl-CoA semialdehyde-lyase (formate-forming). This enzyme catalyses the following chemical reaction
2-hydroxymuconate tautomerase is an enzyme with systematic name (2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase. This enzyme catalyses the following chemical reaction
2-Hydroxymuconate semialdehyde is formed from catechol by the enzyme catechol 2,3-dioxygenase during the degradation of benzoates. It is hydrolysed into formate and 2-oxopent-4-enoate by 2-hydroxymuconate-semialdehyde hydrolase.
2-Oxopent-4-enoic acid (2-oxopent-4-enoate) is formed by the dehydration of 4-hydroxy-2-oxopentanoate by 2-oxopent-4-enoate hydratase or by the hydrolysis of 2-hydroxymuconate semialdehyde by 2-hydroxymuconate-semialdehyde hydrolase.
References
Harayama S, Rekik M, Wasserfallen A, Bairoch A (1987). "Evolutionary relationships between catabolic pathways for aromatics: conservation of gene order and nucleotide sequences of catechol oxidation genes of pWW0 and NAH7 plasmids". MGG Mol. Gen. Genet. 210 (2): 241–247. doi:10.1007/BF00325689. PMID3481421. S2CID20302884.
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