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3.1.1.24

Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida)

Methods Enzymol.

17A

529-549

1970

-

3.1.1.24

Cloning and expression of Acinetobacter calcoaceticus catBCDE genes in Pseudomonas putida and Escherichia coli

J. Bacteriol.

165

557-563

1986

3.1.1.24

Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity

J. Bacteriol.

180

1072-1081

1998

3.1.1.24

The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida

J. Biol. Chem.

241

3787-3794

1966

3.1.1.24

The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida

J. Biol. Chem.

241

3787-3794

1966

3.1.1.24

Evidence for two uptake systems in Rhizobium leguminosarum for hydroxy-aromatic compounds metabolized by the 3-oxoadipate pathway

Arch. Microbiol.

156

385-391

1991

-

3.1.1.24

Modified 3-oxoadipate pathway for the biodegradation of methylaromatics in Pseudomonas reinekei MT1

J. Bacteriol.

192

1543-1552

2010

3.1.1.24

A product analog bound form of 3-oxoadipate-enol-lactonase (PcaD) reveals a multifunctional role for the divergent cap domain

J. Mol. Biol.

406

649-658

2011

3.1.1.24

A multi-faceted analysis of RutD reveals a novel family of alpha/beta hydrolases

Proteins

80

2359-2368

2012

3.1.1.24

In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL the protocatechuate branch of the beta-ketoadipate pathway in Rhodococcus jostii RHA1

Biosci. Biotechnol. Biochem.

79

830-835

2015