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MetaCyc Pathway: catechol degradation III (ortho-cleavage pathway)

Enzyme View:

Pathway diagram: catechol degradation III (ortho-cleavage pathway)

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/AssimilationAromatic Compounds DegradationCatechol 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

Expected Taxonomic Range: Fungi, Proteobacteria

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].

In Pseudomonas putida the enzymes involved in β-ketoadipate degradation ( β-ketoadipate:succinyl CoA transferase, and β-ketoadipyl CoA thiolase) are inducible by 3-oxoadipate [Ornston66].

Superpathways: mandelate degradation to acetyl-CoA

Subpathways: 3-oxoadipate degradation, catechol degradation to β-ketoadipate

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

Created 04-Dec-2006 by Caspi R, SRI International


Chan79: Chan WY, Seale TW, Shukla JB, Rennert OM (1979). "Polyamine conjugates and total polyamine concentrations in human amniotic fluid." Clin Chim Acta 91(3);233-41. PMID: 761399

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

Harwood96: Harwood CS, Parales RE (1996). "The beta-ketoadipate pathway and the biology of self-identity." Annu Rev Microbiol 50;553-90. PMID: 8905091

MacLean06: MacLean AM, MacPherson G, Aneja P, Finan TM (2006). "Characterization of the beta-ketoadipate pathway in Sinorhizobium meliloti." Appl Environ Microbiol 72(8);5403-13. PMID: 16885292

Ornston66: Ornston LN (1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. IV. Regulation." J Biol Chem 241(16);3800-10. PMID: 5916393

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

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

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

Goldman85: Goldman A, Ollis D, Ngai KL, Steitz TA (1985). "Crystal structure of muconate lactonizing enzyme at 6.5 A resolution." J Mol Biol 182(2);353-5. PMID: 3999146

Goldman87: Goldman A, Ollis DL, Steitz TA (1987). "Crystal structure of muconate lactonizing enzyme at 3 A resolution." J Mol Biol 194(1);143-53. PMID: 3612800

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

Katti89: Katti SK, Katz BA, Wyckoff HW (1989). "Crystal structure of muconolactone isomerase at 3.3 A resolution." J Mol Biol 205(3);557-71. PMID: 2926818

Katz85: Katz BA, Ollis D, Wyckoff HW (1985). "Low resolution crystal structure of muconolactone isomerase. A decamer with a 5-fold symmetry axis." J Mol Biol 184(2);311-7. PMID: 4032480

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

Kukor88: Kukor JJ, Olsen RH, Ballou DP (1988). "Cloning and expression of the catA and catBC gene clusters from Pseudomonas aeruginosa PAO." J Bacteriol 170(10);4458-65. PMID: 3139626

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Meagher90: Meagher RB, Ngai KL, Ornston LN (1990). "Muconate cycloisomerase." Methods Enzymol 188;126-30. PMID: 2280697

Meagher90a: Meagher RB, Ngai KL, Ornston LN (1990). "Muconolactone isomerase." Methods Enzymol 188;130-3. PMID: 2280698

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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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc13.