This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: β-ketoadipate pathway
|Superclasses:||Degradation/Utilization/Assimilation → Aromatic Compounds Degradation → Catechol Degradation|
Some taxa known to possess this pathway include : Acinetobacter calcoaceticus, Agrobacterium tumefaciens, Cupriavidus necator, Pseudomonas aeruginosa, Pseudomonas knackmussii, Pseudomonas putida, Pseudomonas putida mt-2, Rhizobium leguminosarum, Rhizobium leguminosarum bv. trifolii, Sinorhizobium meliloti Rm2011, Trichosporon cutaneum
Catechol can be degraded via either of two routes: the meta cleavage pathway (see meta cleavage pathway of aromatic compounds), or the ortho-cleavage pathway (this pathway). When degraded by this pathway, catechol is cleaved between the two ring hydroxyls by the enzyme catechol 1,2-dioxygenase forming cis,cis-muconate, which is then further metabolyzed in three steps to the important intermediate 3-oxoadipate.
3-oxoadipate is a convergence point of the two branches of the β-ketoadipate pathway (see aromatic compounds degradation via β-ketoadipate); one of the branches is this pathway, while the other one starts with protocatechuate (see protocatechuate degradation II (ortho-cleavage pathway). Once β-Ketoadipate is formed, it is converted to succinyl-CoA and acetyl-CoA.
The pathway is widely distributed among soil bacteria and fungi, even though its organization and regulation vary among species [Stanier50, Harwood96, Parke86, MacLean06]. For example, in Pseudomonas putida the genes that encode the regulatory proteins and the enzymes of this pathway are clustered into two distinct groups [Chan79], while in Acinetobacter calcoaceticus they are arranged in a single cluster induced by protocatechuate [Harwood94].
Superpathways: mandelate degradation to acetyl-CoA
Variants: aromatic compounds degradation via β-ketoadipate, catechol degradation I (meta-cleavage pathway), catechol degradation II (meta-cleavage pathway), catechol degradation to 2-oxopent-4-enoate I, catechol degradation to 2-oxopent-4-enoate II
Harwood94: Harwood CS, Nichols NN, Kim MK, Ditty JL, Parales RE (1994). "Identification of the pcaRKF gene cluster from Pseudomonas putida: involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate." J Bacteriol 176(21);6479-88. PMID: 7961399
Parke86: Parke D, Ornston LN (1986). "Enzymes of the beta-ketoadipate pathway are inducible in Rhizobium and Agrobacterium spp. and constitutive in Bradyrhizobium spp." J Bacteriol 165(1);288-92. PMID: 3941043
Stanier50: Stanier, R.Y., Sleeper, B.P., Tsuchida, M., MacDonald, D.L. (1950). "The bacterial oxidation of aromatic compounds; III. The enzymatic oxidation of catechol and protocatechuic acid to beta-ketoadipic acid." J Bacteriol 59(2): 137-151. PMID: 15421941
Aldrich87: Aldrich TL, Frantz B, Gill JF, Kilbane JJ, Chakrabarty AM (1987). "Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme." Gene 52(2-3);185-95. PMID: 3609743
Aldrich88: Aldrich TL, Chakrabarty AM (1988). "Transcriptional regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida." J Bacteriol 170(3);1297-304. PMID: 2449420
Camara07: Camara B, Bielecki P, Kaminski F, dos Santos VM, Plumeier I, Nikodem P, Pieper DH (2007). "A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate." J Bacteriol 189(5);1664-74. PMID: 17172348
Dorn78: Dorn E, Knackmuss HJ (1978). "Chemical structure and biodegradability of halogenated aromatic compounds. Two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad." Biochem J 174(1);73-84. PMID: 697765
Ferrandez98: Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E (1998). "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." J Biol Chem 1998;273(40);25974-86. PMID: 9748275
Ismail03: Ismail W, El-Said Mohamed M, Wanner BL, Datsenko KA, Eisenreich W, Rohdich F, Bacher A, Fuchs G (2003). "Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli." Eur J Biochem 270(14);3047-54. PMID: 12846838
Kaschabek02: Kaschabek SR, Kuhn B, Muller D, Schmidt E, Reineke W (2002). "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase." J Bacteriol 184(1);207-15. PMID: 11741862
Kojima67: Kojima Y, Fujisawa H, Nakazawa A, Nakazawa T, Kanetsuna F, Taniuchi H, Nozaki M, Hayaishi O (1967). "Studies on pyrocatechase. I. Purification and spectral properties." J Biol Chem 242(14);3270-8. PMID: 6029438
McCorkle80: McCorkle GM, Yeh WK, Fletcher P, Ornston LN (1980). "Repetitions in the NH2-terminal amino acid sequence of beta-ketoadipate enol-lactone hydrolase from Pseudomonas putida." J Biol Chem 255(13);6335-41. PMID: 7391022
Nakai88: Nakai C, Nakazawa T, Nozaki M (1988). "Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1." Arch Biochem Biophys 267(2);701-13. PMID: 3214177
Nakai90: Nakai C, Horiike K, Kuramitsu S, Kagamiyama H, Nozaki M (1990). "Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), alpha alpha, alpha beta, and beta beta, from Pseudomonas arvilla C-1." J Biol Chem 265(2);660-5. PMID: 2295613
Nakai95: Nakai C, Uyeyama H, Kagamiyama H, Nakazawa T, Inouye S, Kishi F, Nakazawa A, Nozaki M (1995). "Cloning, DNA sequencing, and amino acid sequencing of catechol 1,2-dioxygenases (pyrocatechase) from Pseudomonas putida mt-2 and Pseudomonas arvilla C-1." Arch Biochem Biophys 321(2);353-62. PMID: 7646060
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