Novel aerobic 2‐aminobenzoate metabolism

Altenschmidt, Uwe; Fuchs, Georg

doi:10.1111/j.1432-1033.1992.tb16835.x

Cited by 43 publications

(28 citation statements)

References 33 publications

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“…strain SU and Pseudomonas sp. strain CBS-3, respectively (8,44), and 20% identical to a coumarateCoA ligase from parsley and a 4-aminobenzoate-CoA ligase from Pseudomonas strain KB740 (2,36). A comparable degree of similarity was seen with several acetate-CoA ligases.…”

Section: Resultssupporting

confidence: 49%

“…4), failed to reveal any stretches that could be construed as characteristic of an aromatic acid subgroup of CoA ligases. However, withi the exception of the 2-aminobenzoate-CoA ligase sequence (2), all the aromatic acid CoA ligases have in common a short stretch of sequence, (T,S)SGTTG(L,X)PKG, that has been proposed by Babbitt et al (8) as an amino acid sequence motif involved in acyl-adenylate formation. It is possible that some clearer relationships among these proteins will become apparent when more sequences of ligases involved in anaerobic catabolic pathways become available.…”

Section: Discussionmentioning

confidence: 99%

“…Support for this suggestion comes from the observation that the very high aromatic acid substrate affinity (<1 ,uM) of the benzoate-CoA ligase (22) matches the high affinity benzoate-CoA ligase fromArthrobacter sp. strain SU ( [44]), 4-coumarate-CoA ligase from parsley (couI acid-CoA ligase from E. coli (f.a.lig [10]), acetyl-CoA M. soehngenii (Meth.acet.lig [20]), acetyl-CoA syn crassa (Neur.acet.lig [15]), E. coli enterobactin synth E (ent.syn.E [47]), R. palustris 4-HBA-CoA ligase report]), and 2-aminobenzoate-CoA ligase from i strain KB740 (2AB.lig [2] (3,52) and attributed to the presence of inhibitors. (38).…”

Section: Discussionmentioning

confidence: 99%

“…Mailing address: Section of Biochemistry, Molecular and Cell Biology, Biotechnology Building, Cornell University, Ithaca, NY 14853. Phone: (607) 255-2432. ically in aerobic aromatic acid metabolism have been purified (2,4,14,35,37), and the genes encoding some of these enzymes have been cloned and sequenced (2,8,44).…”

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confidence: 99%

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4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation

et al. 1994

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Anaerobic metabolism of most aromatic acids is initiated by coenzyme A thioester formation. Rhodopseudomonas palustris grows well under anaerobic, phototrophic conditions with many aromatic acids, including benzoate and 4-hydroxybenzoate, as a carbon source. A coenzyme A ligase that reacts with 4-hydroxybenzoate was purified from 4-hydroxybenzoate-grown cells of R. palustris. This enzyme required MgATP, reduced coenzyme A, and 4-hydroxybenzoate, benzoate, or cyclohex-1,4-dienecarboxylate for optimal activity but also used phosphopantetheine, cyclohex-2,5-dienecarboxylate, and 4-fluorobenzoate at lower rates. The 4-hydroxybenzoate-coenzyme A ligase differed in molecular characteristics from a previously described benzoate-coenzyme A ligase from R. palustris, and the two ligases did not cross-react immunologically. The gene encoding the 4-hydroxybenzoate enzyme was cloned and sequenced. The deduced gene product showed about 20% amino acid identity with bacterial coenzyme A ligases involved in aerobic degradation of aromatic acids. An R. palustris mutant carrying a disrupted 4-hydroxybenzoate-coenzyme A ligase gene was unable to grow with 4-hydroxybenzoate under anaerobic conditions, indicating that the enzyme is essential for anaerobic degradation of this compound.

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Section: Resultssupporting

confidence: 49%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation

et al. 1994

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“…The enzyme of 130 kDa composed of two identical subunits of 56 kDa was purified and characterized. Cells grown aerobically with 3-hydroxybenzoate contained a similarly active CoA ligase for 3-hydroxybenzoate, 3 Microorganisms degrade aromatic compounds by two different principles; both are used by facultative anaerobic microorganisms. Under anaerobic conditions, the aromatic ring structures are attacked reductively and several central intermediates are formed (for a review, see reference 15).…”

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confidence: 99%

New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp

et al. 1993

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A denitrifying Pseudomonas sp. is able to oxidize aromatic compounds compounds completely to CO2, both aerobically and anaerobically. It is shown that benzoate is aerobically oxidized by a new degradation pathway via benzoyl-coenzyme A (CoA) and 3-hydroxybenzoyl-CoA. The organism grew aerobically with benzoate, 3-hydroxybenzoate, and gentisate; catechol, 2-hydroxybenzoate, and protocatechuate were not used, and 4-hydroxybenzoate was a poor substrate. Mutants were obtained which were not able to utilize benzoate as the sole carbon source aerobically but still used 3-hydroxybenzoate or gentisate. Simultaneous adaptation experiments with whole cells seemingly suggested a sequential induction of enzymes of a benzoate oxidation pathway via 3-hydroxybenzoate and gentisate. Cells grown aerobically with benzoate contained a benzoate-CoA ligase (AMP forming) (0.1 mumol min-1 mg-1) which converted benzoate but not 3-hydroxybenzoate into its CoA thioester. The enzyme of 130 kDa composed of two identical subunits of 56 kDa was purified and characterized. Cells grown aerobically with 3-hydroxybenzoate contained a similarly active CoA ligase for 3-hydroxybenzoate, 3-hydroxybenzoate-CoA ligase (AMP forming). Extracts from cells grown aerobically with benzoate catalyzed a benzoyl-CoA- and flavin adenine dinucleotide-dependent oxidation of NADPH with a specific activity of at least 25 nmol NADPH oxidized min-1 mg of protein-1; NADH and benzoate were not used. This new enzyme, benzoyl-CoA 3-monooxygenase, was specifically induced during aerobic growth with benzoate and converted [U-14C]benzoyl-CoA stoichiometrically to [14C]3-hydroxybenzoyl-CoA.

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Degradation of Aromatic Compounds by Nonsulfur Purple Bacteria

Gibson

Harwood

Advances in Photosynthesis and Respiration

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Novel aerobic 2‐aminobenzoate metabolism

Cited by 43 publications

References 33 publications

4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation

4-Hydroxybenzoate-coenzyme A ligase from Rhodopseudomonas palustris: purification, gene sequence, and role in anaerobic degradation

New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp

Degradation of Aromatic Compounds by Nonsulfur Purple Bacteria

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