trans-o-Hydroxybenzylidenepyruvate hydratase-aldolase as a biocatalyst.

Organization and Evolution of Naphthalene Catabolic Pathways: Sequence of the DNA Encoding 2-Hydroxychromene-2-Carboxylate Isomerase and trans-o-Hydroxybenzylidenepyruvate Hydratase-Aldolase from the NAH7 Plasmidt

The sequence of a 2,437-bp DNA segment from the naphthalene upper catabolic pathway operon of plasmid NAH7 was determined. This segment contains three large open reading frames designated nahQ', nahE, and nahD. The first of these is the 3' end of an open reading frame that has no known function, the second (993 bp) encodes trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (deduced molecular...

Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway.

From a soil isolate, Pseudomonas strain C18, we cloned and sequenced a 9.8-kb DNA fragment that encodes dibenzothiophene-degrading enzymes. Nine open reading frames were identified and designated doxABDEFGHIJ. Collectively, we refer to these genes as the DOX pathway. At the nucleotide level, doxABD are identical to the ndoABC genes that encode naphthalene dioxygenase of Pseudomonas putida. The ...

Isolation of a thermophilic bacterium, Geobacillus sp. SH-1, capable of degrading aliphatic hydrocarbons and naphthalene simultaneously, and identification of its naphthalene degrading pathway.

A thermophilic naphthalene- and aliphatic hydrocarbon-degrading bacterium SH-1 was isolated from a deep oil well and identified as Geobacillus sp. n-alkanes from C12 to C33 in crude oil and naphthalene were effectively degraded by strain SH-1, and this strain could readily utilize these compounds as its sole carbon and energy resources. During the degradation of naphthalene, strain SH-1 initiat...

Stereospecific enzymes in the degradation of aromatic compounds by pseudomonas putida.

Two reactions in the catabolism of catechol by meta-fission, namely, hydration of 2-oxopent-4-enoate (vinylpyruvate) and aldol fission of the product, are catalyzed by stereospecific enzymes. The absolute configuration of this hydration product was shown to be l(S)-4-hydroxy-2-oxopentanoate. Vinylpyruvate hydratase, purified almost to homogeneity, had a molecular weight of about 287,000 and was...

Organic Solvent Tetralin Aldolase Involved in Biodegradation of the Identification of a Hydratase and a Class II