Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase

Freudenberg, W.

doi:10.1016/0378-1097(88)90293-5

Cited by 23 publications

(29 citation statements)

References 13 publications

(20 reference statements)

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“…Close inspection of the data (23) indicates that the enzyme exhibits a small peak at 411 nm indicative of a cytochrome, which also might have been lost. Formation of the hydroxylated intermediate seems to be quite similar to the hydroxylation of N-heterocyclic compounds such as purines (4), nicotine (13), nicotinic acid (11,34), or picolinic acid (44), as noted before (23). A relationship of the two reactions is indicated by the observed unspecificity of XDH for 2-furoylCoA, as observed in our strain P. putida Ful (24).…”

Section: Discussionsupporting

confidence: 76%

Xanthine dehydrogenase and 2-furoyl-coenzyme A dehydrogenase from Pseudomonas putida Fu1: two molybdenum-containing dehydrogenases of novel structural composition

Koenig

Andreesen

1990

J Bacteriol

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The constitutive xanthine dehydrogenase and the inducible 2-furoyl-coenzyme A (CoA) dehydrogenase could be labeled with ['85W]tungstate. This labeling was used as a reporter to purify both labile proteins. The radioactivity cochromatographed predominantly with the residual enzymatic activity of both enzymes during the first purification steps. Both radioactive proteins were separated and purified to homogeneity. Antibodies raised against the larger protein also exhibited cross-reactivity toward the second smaller protein and removed xanthine dehydrogenase and 2-furoyl-CoA dehydrogenase activity up to 80 and 60% from the supernatant of cell extracts, respectively. With use of cell extract, Western immunoblots showed only two bands which correlated exactly with the activity stains for both enzymes after native polyacrylamide gel electrophoresis. Molybdate was absolutely required for incorporation of '85W, formation of cross-reacting material, and enzymatic activity. The latter parameters showed a perfect correlation. This evidence proves that the radioactive proteins were actually xanthine dehydrogenase and 2-furoyl-CoA dehydrogenase. The apparent molecular weight of the native xanthine dehydrogenase was about 300,000, and that of 2-furoyl-CoA dehydrogenase was 150,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of both enzymes revealed two protein bands corresponding to molecular weights of 55,000 and 25,000. The xanthine dehydrogenase contained at least 1.6 mol of molybdenum, 0.9 ml of cytochrome b, 5.8 mol of iron, and 2.4 mol of labile sulfur per mol of enzyme. The composition of the 2-furoyl-CoA dehydrogenase seemed to be similar, although the stoichiometry was not determined. The oxidation of furfuryl alcohol to furfural and further to 2-furoic acid by Pseudomonas putida Ful was catalyzed by two different dehydrogenases.Pseudomonas putida Ful was isolated from an enrichment culture with 2-furoic acid as the sole source of carbon and energy (24). The formation of 2-furoyl-coenzyme A (CoA) is the first reaction step in 2-furoic acid degradation. The second enzymatic step is catalyzed by a dehydrogenase that introduces a hydroxyl group to form 5-hydroxy-2-furoylCoA (23,24,49,50). Other substrates for P. putida Ful were furfuryl alcohol and furfural, which were degraded via 2-furoic acid and 2-furoyl-CoA (Fig.

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Section: Discussionsupporting

confidence: 76%

Xanthine dehydrogenase and 2-furoyl-coenzyme A dehydrogenase from Pseudomonas putida Fu1: two molybdenum-containing dehydrogenases of novel structural composition

Koenig

Andreesen

1990

J Bacteriol

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“…Rather, it suggests that the formyl group is dehydrogenated while still bound to the primary amino group of methanofuran yielding N-carboxymethanofuran as product (reaction b) which should break down non-enzymically to CO, and methanofuran (Ewing et al, 1980) : 0 R Reaction (b) indicates that formylmethanofuran dehydrogenase belongs to the group of molybdenum enzymes that catalyze an insertion of an oxygen atom derived from H,O into a C-H bond (Pilato and Stiefel, 1993). Enzymes belonging to this group are xanthine dehydrogenases and xanthine oxidases (Bray, 1988;Wootton et al, 1991), molybdenum-containing formate dehydrogenases (Adams and Mortenson, 1985;Barber et al, 1986;Friedebold and Bowien, 1993), formate-ester dehydrogenase (van Ophem et al, 1992), aldehyde oxidase (Branzoli and Massey, 1974), aldehyde dehydrogenase (Poels et al, 1987), aldehyde oxidoreductase (White et al, 1993), nicotine dehydrogenase (Freudenberg et al, 1988), nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase (Nagel and Andreesen, 1990), isonicotinate dehydrogenase and 2-hydroxyisonicotinate dehydrogenase (Kretzer and Andreesen, 1991), quinoline oxidoreductase (Hettrich et al, 1991), quinoline-4-carboxylic acid oxidoreductase (Bauer and Lingens, 19921, quinaldine oxidoreductase (de Beyer and Lingens, 1993), quinaldic acid 4-oxidoreductase (Fetzner and Lingens, 1993), picolinate dehydrogenase (Siegmund et al, 1990), 2-furoyl-coenzyme A dehydrogenase , and pyrimidine oxidase and pyridoxal oxidase (Burgmayer and Stiefel, 1985). Interestingly, one of these enzymes, milk xanthine oxidase, can even catalyze the dehydrogenation of formamide to carbamic acid (Morpeth et al, 1984) which is a reaction also catalyzed by formylrnethanofuran dehydrogenase.…”

Section: Discussionmentioning

confidence: 99%

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Bertram

Karrasch

Schmitz

et al. 1994

European Journal of Biochemistry

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Formylmethanofuran dehydrogenases, which are found in methanogenic Archaea, are molybdenum or tungsten iron-sulfur proteins containing a pterin cofactor. We report here on differences in substrate specificity, EPR properties and susceptibility towards cyanide inactivation of the enzymes from Methanosarcina barkeri, Methanobacterium thermoautotrophicum and Methanobacterium woljei.The molybdenum enzyme from M. barkeri (relative activity with N-formylmethanofuran = 100%) was found to catalyze, albeit at considerably reduced apparent V,,,,,, the dehydrogenation of N-furfurylformamide (11 %), N-methylformamide (0.2%), formamide (0.1 %) and formate (1 %). The molybdenum enzyme from M. wolfei could only use N-furfurylformamide (1 %) and formate (3 %) as pseudosubstrates. The molybdenum enzyme from M. thermoautotrophicum and the tungsten enzymes from M. thermoautotrophicum and M. wolfei were specific for N-formylmethanofuran.The molybdenum formylmethanofuran dehydrogenases exhibited at 77 K two rhombic EPR signals, designated FMDred and FMD,,, both derived from Mo as shown by isotopic substitution with 9 7 M~. The FMD,, signal was only displayed by the active enzyme in the reduced form and was lost upon enzyme oxidation; the FMD,, signal was displayed by an inactive form and was not quenched by 0,. The tungsten isoenzymes were EPR silent.The molybdenum formylmethanofuran dehydrogenases were found to be inactivated by cyanide whereas the tungsten isoenzymes, under the same conditions, were not inactivated. Inactivation was associated with a characteristic change in the molybdenum-derived EPR signal. Reactivation was possible in the presence of sulfide. Abbreviations. FMD,,,, EPR signal attributed to active formylmethanofuran dehydrogenase ; FMD,,, EPR signal attributed to inactive formylmethanofuran dehydrogenase ; R, Land6 splittina + co2 t P IE" = -497 mV (Thauer, 1990) factor; gx, gy-and g,, Land6 splitting factors in the x , y and directions for anisotropic systems; 1 U = 1 Fmol formylmethanofuran dehydrogenatedmin.The physiological electron accePtor/donor is not knownMethylviologen (E"' = -446 mV) can be used as artificial

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“…1. The nicotine-hydroxylating enzymes, known as nicotine dehydrogenase (NDH) and ketone dehydrogenase (KDH) (8,20), belong to the family of molybdenum cofactor, Fe-S cluster, and flavin adenine dinucleotide (FAD)-dependent hydroxylases (11). 6-Hydroxynicotine oxidases-one specific for 6HLNO and one specific for 6-hydroxy-D-nicotine, a minor side product of nicotine metabolism-are FAD-containing enzymes (5).…”

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confidence: 99%

An α/β-Fold C—C Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

Sachelaru¹,

Schiltz²,

Igloi

et al. 2005

J Bacteriol

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Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase

Cited by 23 publications

References 13 publications

Xanthine dehydrogenase and 2-furoyl-coenzyme A dehydrogenase from Pseudomonas putida Fu1: two molybdenum-containing dehydrogenases of novel structural composition

Xanthine dehydrogenase and 2-furoyl-coenzyme A dehydrogenase from Pseudomonas putida Fu1: two molybdenum-containing dehydrogenases of novel structural composition

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

An α/β-Fold C—C Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

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