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Degradation of benzoate via benzoyl-coenzyme A and gentisate by Bacillus stearothermophilus PK1, and purification of gentisate 1,2-dioxygenase (1996)

Kiemer, P. ; Tshisuaka, B. ; Fetzner, S. ; [et al.]

Springer

Biology and fertility of soils 23 (1996), S. 307-313

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ISSN: 1432-0789

Keywords: Key wordsBacillus stearothermophilus ; Benzoate ; degradation ; Benzoyl-coenzyme A ; Gentisate 1 ; 2-dioxygenase ; Thermophils

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition

Notes: Abstract The thermophilic Bacillus stearothermophilus PK1 utilized benzoate, 3-hydroxybenzoate, and gentisate as sole source of carbon and energy. 2- and 4-Hydroxybenzoate, 2,3- and 3,4-dihydroxybenzoate, and catechol did not support growth. Degradation of benzoate proceeded via benzoyl-coenzyme A (benzoyl-CoA) and gentisate. The inducible benzoyl-CoA ligase converted benzoate but not 3-hydroxybenzoate to its coenzyme A thioester. Gentisate 1,2-dioxygenase from B. stearothermophilus PK1 was purified to homogeneity. The enzyme is presumed to be a homohexamer with a subunit molecular mass of 40 kDa. It showed maximal activity at 65–70°C. After incubation for 80 min at 65°C, 50% of the original activity was lost. Gentisate 1,2-dioxygenase activity from strain PK1 was strictly dependent on exogenously added Fe2+, and it was inhibited by metal-chelating agents, indicating an essential role of Fe2+ in catalysis.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00335959

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The Biosynthesis of Aromatic Amino Acids and its Regulation (1968)

Lingens, F.

Weinheim : Wiley-Blackwell

Angewandte Chemie International Edition in English 7 (1968), S. 350-360

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ISSN: 0570-0833

Keywords: Biosynthesis ; Amino acids ; Shikimic acid ; Chemistry ; General Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: Microorganisms synthesize the aromatic amino acids phenylalanine, tyrosine, and tryptophan, as well as the related compounds p-aminobenzoic acid, tetrahydrofolic acid, p-hydroxybenzoic acid, ubiquinone, vitamin K, and nicotinic acid, by a highly branched route passing through shikimic acid. The biosynthesis is not regulated in the same way in all the organisms studied. The regulation is strongly dependent on the ability of the enzymes involved to be resolved into isozymes, their ability to be inhibited, and their activation, repression, and induction.