The hydroxylation of nicotinic acid by <i>Pseudomonas fluorescens</i>

Hunt, Angela; Hughes, D. E.; Lowenstein, John M.

doi:10.1042/bj0690170

Cited by 71 publications

(27 citation statements)

References 13 publications

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“…The incorporated hydroxyl group is derived from water (Hunt et al, 1958;Hirschberg & Ensign, 1971;Pereira et al, 1988 ;Bray, 1988). These dehydrogenases which hydroxylate pyridine derivatives at the ortho-position form a structurally very similar group of molybdoenzymes.…”

Section: Introductionmentioning

confidence: 99%

Catabolism of isonicotinate by Mycobacterium sp. INA1: extended description of the pathway and purification of the molybdoenzyme isonicotinate dehydrogenase

Kretzer

Frunzke

Andreesen

1993

Journal of General Microbiology

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Catabolism of isonicotinate by Mycobucterium sp. INAl has been shown to proceed via 2-hydroxyisonicotinate, 2,6-dihydroxyisonicotinate (citrazinate), citrazyl-CoA and 2,6-dioxopiperidine-4-carboxyl-CoA. An extended pathway involving propane-1,2,3-tricarboxylate as a further intermediate is presented in this paper. Propane-1,2,3-tricarboxylate was oxidized stepwise to 2-oxoglutarate involving an oxidase, aconitase and isocitrate dehydrogenase. Isonicotinate dehydrogenase catalyses the first step of isonicotinate metabolism in Mycobacterium sp. INA1. The enzyme was purified to apparent homogeneity by a three-step procedure. Enrichment was accompanied by partial loss in specific activity. The native enzyme had a molecular mass of either 125 kDa or 250 kDa, when estimated by native gradient PAGE or gel filtration, respectively. SDS-gel electrophoresis revealed three types of subunits with molecular masses of approximately 83, 31 and 19 kDa. N-Terminal amino acid sequences of all three subunits have been determined. Molybdenum, iron, acid-labile sulphur and FAD were present at molar ratios of 1, 4, 4, 1 per protomer (125 kDa). The molybdenum-complexing cofactor was shown to be molybdopterin cytosine dinucleotide. Besides isonicotinate, only quinoline-4carboxylate was found to be oxidized at appreciable rates.

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Section: Introductionmentioning

confidence: 99%

Catabolism of isonicotinate by Mycobacterium sp. INA1: extended description of the pathway and purification of the molybdoenzyme isonicotinate dehydrogenase

Kretzer

Frunzke

Andreesen

1993

Journal of General Microbiology

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“…It occurs, for example, in the degradation of nicotinate (Hughes, 1955), picolinate (Dagley & Johnson, 1963), nicotine (Hochstein & Rittenberg, 1959), quinoline (Grant & Al-Najjar, 1976), furan-2-carboxylate (Trudgill, 1969), and thiophene-2-carboxylate (Cripps, 1973). Further common features of these reactions seem to be that the incorporated hydroxyl group is derived from water but not from oxygen (Hunt et al, 1958 ;Hirschberg & Ensign, 1959;Pereira et al, 1988) and that they are affected by the availability of molybdate Siegmund et al, 1990). Several of the dehydrogenases involved have been shown to contain a molybdenum cofactor (Kruger et al, 1987;Freudenberg et al, 1988;.…”

Section: Discussionmentioning

confidence: 99%

A new pathway for isonicotinate degradation by Mycobacterium sp. INA1

Kretzer

Andreesen

1991

Journal of General Microbiology

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An organism able to utilize isonicotinate aerobically as the sole source of carbon, nitrogen and energy was isolated from soil samples and identified as a Mycobucterium sp. No growth occurred on any other heteroaromatic substrate tested, except 2-hydroxyisonicotinate, which was shown to be an intermediate in isonicotinate metabolism. Degradation of isonicotinate involved two consecutive hydroxylations leading to 2,6-dihydroxyisonicotinate (citrazinate). The reactions were catalysed by two different dehydrogenases, which were apparently molybdenum-dependent. Citrazinate was activated by CoA via a synthetase reaction, and the resulting citrazylCoA ester was reduced by a NADPH-dependent reductase. In the presence of 1 mM-arsenite, cells accumulated 2-oxoglutarate during isonicotinate metabolism.

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“…In bacteria, hydroxylation of nicotinate is catalyzed by nicotinate hydroxylase (Hunt et al 1958;Hunt 1959). Oxygen tracing studies have demonstrated that the O in the hydroxyl group comes from H 2 O not O 2 (Hunt et al 1958;Ensign 1971a, b, 1972), thus the enzyme was renamed nicotinate dehydrogenase (Amano et al 2007;Andreesen and Fetzner 2002;Nagel and Andreesen 1989).…”

Section: Introductionmentioning

confidence: 98%

Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440

et al. 2009

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6-hydroxynicotinate can be used for the production of drugs, pesticides and intermediate chemicals. Some Pseudomonas species were reported to be able to convert nicotinic acid to 6-hydroxynicotinate by nicotinate dehydrogenase. So far, previous reports on NaDH in Pseudomonas genus were confused and contradictory each other. Recently, Ashraf et al. reported an NaDH gene cloned from Eubacterium barkeri and suggested some deducted NaDH genes from other nine bacteria. But they did not demonstrate the activity of recombinant NaDH and did not mention NaDH gene in Pseudomonas. In this study we cloned the gene of NaDH, ndhSL, from Pseudomonas putida KT2440. NdhSL in P. putida KT2440 is composed of two subunits. The small subunit contains [2Fe2S] iron sulfur domain, while the large subunit contains domains of molybdenum cofactor and cytochrome c. Expression of recombinant ndhSL in P. entomophila L48, which lacks the ability to produce 6-hydroxynicotinate, enabled the resting cell and cell extract of engineering P. entomophila L48 to hydroxylate nicotinate. Gene knockout and recovery studies further confirmed the ndhSL function.

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The hydroxylation of nicotinic acid by Pseudomonas fluorescens

Cited by 71 publications

References 13 publications

Catabolism of isonicotinate by Mycobacterium sp. INA1: extended description of the pathway and purification of the molybdoenzyme isonicotinate dehydrogenase

Catabolism of isonicotinate by Mycobacterium sp. INA1: extended description of the pathway and purification of the molybdoenzyme isonicotinate dehydrogenase

A new pathway for isonicotinate degradation by Mycobacterium sp. INA1

Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440

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