Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species.

doi:10.1111/J.1432-1033.1993.TB17794.X

Paper

Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species.

Published Apr 1, 1993 · T. Biegert, U. Altenschmidt, C. Eckerskorn

European journal of biochemistry

Q1 SJR score

78

Citations

2

Influential Citations

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Abstract

The initial step of anaerobic 4-hydroxybenzoate and 3-hydroxybenzoate degradation was studied in a denitrifying Pseudomonas sp. 4'-Hydroxybenzoate and 3-hydroxybenzoate are converted into their coenzyme A (CoA) thioesters by two different specific coenzyme A ligases. 4-Hydroxybenzoate-CoA ligase (AMP-forming) was purified 350-fold. The ligase is active as a monomer of molecular mass 48 kDa, as determined by gel filtration and SDS/PAGE. At a pH optimum of 8.5, the apparent Km values for 4-hydroxybenzoate, ATP, and coenzyme A are 37 microM, 77 microM, and 125 microM, respectively. The enzyme reacts specifically with 4-hydroxybenzoate (100%) and 4-aminobenzoate (30%). Other analogues of benzoate, notably 3- or 2-hydroxybenzoate, are inactive, and 2,4-dihydroxybenzoate and 2-hydroxy-4-methylbenzoate act as competitive inhibitors (Ki = 1 microM). Polyclonal antibodies were raised and used in immunoblot assays to study the regulation of the expression of 4-hydroxybenzoate-CoA ligase. The ligase is synthesized when cells are grown anaerobically with 4-hydroxybenzoate, phenol, or p-cresol; phenol and p-cresol are degraded via 4-hydroxybenzoate. The enzyme is not present in cells grown aerobically with 4-hydroxybenzoate or anaerobically with benzoate or 4-hydroxyphenylacetate.

In Vitro Study

Highly Cited

Study Snapshot

The 4-hydroxybenzoate-CoA ligase plays a crucial role in anaerobic metabolism of phenolic compounds, enabling the degradation of phenol and p-cresol in denitrifying Pseudomonas species.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species.

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References

Citations

Characterization of 2-phenanthroate:CoA ligase from the sulfate-reducing, phenanthrene-degrading enrichment culture TRIP

The 2-phenanthroate:CoA ligase plays a crucial role in the anaerobic degradation of polycyclic aromatic hydrocarbons like phenanthrene, with optimal activity at pH 7.5 and oxygen-insensitivity.

Sensitive and selective phenol sensing in denitrifying Aromatoleum aromaticum EbN1T

Aromatoleum aromaticum EbN1T has highly selective sensing for phenol, p-cresol, and p-ethylphenol, making it a valuable tool for understanding and promoting biodegradation of aromatic compounds.

Monolignol acyltransferase for lignin p-hydroxybenzoylation in Populus

PHBMT1 is a key enzyme in Populus plants that controls p-hydroxybenzoylation, which alters lignin structure and physiochemical properties, offering potential for tailoring woody biomass.

Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily

Aryl-coenzyme A (CoA) ligases catalyze thioester bonds between aromatic compounds and CoA, and may be the ancestral proteins from which all other ANL superfamily enzymes developed.

Gas ebullition from petroleum hydrocarbons in aquatic sediments: A review.

Short-chain C 10 alkanes are the only petroleum hydrocarbon class that can potentially drive gas ebullition in sediments, with methanogenesis playing a minor role compared to natural organic matter.