p-Nitrosophenol Reduction by Liver Cytosol from ADH-Positive and -Negative Deermice (Peromyscus maniculatus)

Dudley, Billy F.; Winston, Gary W.

doi:10.1006/abbi.1995.1118

Cited by 5 publications

(5 citation statements)

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“…We know that benzaldehyde is a substrate for both AOX1 and AOH1, and this substrate forms the basis of an electrophoretic assay which is used to measure the two enzymes [10,14,49]. The oxidase activity of AOX1 is inhibited by compounds such as dicoumarol [50] or methadone [51], although the specificity of the two inhibitors for the enzyme is questionable.…”

Section: Figure 1 Domain Composition Of a Prototypical Mfementioning

confidence: 99%

Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology

Garattini

Mendel

Romão

et al. 2003

Biochemical Journal

219

228

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The molybdo-flavoenzymes are structurally related proteins that require a molybdopterin cofactor and FAD for their catalytic activity. In mammals, four enzymes are known: xanthine oxidoreductase, aldehyde oxidase and two recently described mouse proteins known as aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2. The present review article summarizes current knowledge on the structure, enzymology, genetics, regulation and pathophysiology of mammalian molybdo-flavoenzymes. Molybdo-flavoenzymes are structurally complex oxidoreductases with an equally complex mechanism of catalysis. Our knowledge has greatly increased due to the recent crystallization of two xanthine oxidoreductases and the determination of the amino acid sequences of many members of the family. The evolution of molybdo-flavoenzymes can now be traced, given the availability of the structures of the corresponding genes in many organisms. The genes coding for molybdo-flavoenzymes are expressed in a cell-specific fashion and are controlled by endogenous and exogenous stimuli. The recent cloning of the genes involved in the biosynthesis of the molybdenum cofactor has increased our knowledge on the assembly of the apo-forms of molybdo-flavoproteins into the corresponding holo-forms. Xanthine oxidoreductase is the key enzyme in the catabolism of purines, although recent data suggest that the physiological function of this enzyme is more complex than previously assumed. The enzyme has been implicated in such diverse pathological situations as organ ischaemia, inflammation and infection. At present, very little is known about the pathophysiological relevance of aldehyde oxidase, aldehyde oxidase homologue 1 and aldehyde oxidase homologue 2, which do not as yet have an accepted endogenous substrate.

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Section: Figure 1 Domain Composition Of a Prototypical Mfementioning

confidence: 99%

Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology

Garattini

Mendel

Romão

et al. 2003

Biochemical Journal

219

228

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“…Metabolism of SMX to SMX-HA by CYP2C9/CYP2C8/MPO ,, , reduction of SMX-HA to SMX by NADH cytochrome b5 reductase and cytochrome b5 , autoxidation of SMX-HA to sulfamethoxazole nitroso (SMX-NO) , nonenzymic conjugation of SMX-NO with thiols , and reduction of SMX-NO to SMX-HA by cytosolic reductases .…”

Section: Introductionmentioning

confidence: 99%

“…Reduction of SMX-NO to SMX-HA in mononuclear leucocytes occurs via reaction with glutathione (GSH) and ascorbate . Enzymatic reduction of SMX-NO has not been reported, but rodent liver cytosol contains reductases that are active against p -nitrosophenol . This enzymatic and nonenzymatic reduction allows for the possibility that N 4 -oxidation metabolites are capable of cycling, generating reactive oxygen species, and leading to the oxidation of GSH to glutathione disulfide (GSSG), and subsequently, to toxicity ,,,− .…”

Section: Introductionmentioning

confidence: 99%

Multiple Adduction Reactions of Nitroso Sulfamethoxazole with Cysteinyl Residues of Peptides and Proteins: Implications for Hapten Formation

Callan

Jenkins

Maggs

et al. 2009

Chem. Res. Toxicol.

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Sulfamethoxazole (SMX) induces immunoallergic reactions that are thought to be a result of intracellular protein haptenation by its nitroso metabolite (SMX-NO mass, 267 amu). SMX-NO reacts with protein thiols in vitro, but the conjugates have not been defined chemically. The reactions of SMX-NO with glutathione (GSH), a synthetic peptide (DS3), and two model proteins, human GSH S-transferase pi (GSTP) and serum albumin (HSA), were investigated by mass spectrometry. SMX-NO formed a semimercaptal (N-hydroxysulfenamide) conjugate with GSH that rearranged rapidly (1-5 min) to a sulfinamide. Reaction of SMX-NO with DS3 also yielded a sulfinamide adduct (mass increment, 267 amu) on the cysteine residue. GSTP was exclusively modified at the reactive Cys47 by SMX-NO and exhibited mass increments of 267, 283, and 299 amu, indicative of sulfinamide, N-hydroxysulfinamide, and N-hydroxysulfonamide adducts, respectively. HSA was modified at Cys34, forming only the N-hydroxysulfinamide adduct. HSA modification by SMX-NO under these conditions was confirmed with ELISA and immunoblotting with an antisulfonamide antibody. It is proposed that cysteine-linked N-hydroxysulfinamide and N-hydroxysulfonamide adducts of SMX are formed via the reaction of SMX-NO with cysteinyl sulfoxy acids. Evidence for a multistep assembly of model sulfonamide epitopes on GSH and polypeptides via hydrolyzable intermediates is also presented. In summary, novel, complex, and metastable haptenic structures have been identified on proteins exposed in vitro to the nitroso metabolite of SMX.

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“…, than any other group of small mammals (King 1968;Kirkland and Layne 1989). Members of the genus Peromyscus are model organisms for studies in ecology (Kaufman and Kaufman 1989), behavior (Wolff 1989), physiology (MacMillen and Garland 1989), reproductive and developmental biology (Millar 1989), biochemistry (Alderman et al 1987;Dudley and Winston 1995;Zheng et al 1993), chromosomal evolution (Committee for Standardization of Chromosomes of Peromyscus 1977Peromyscus , 1994Robbins and Baker 1981;Rogers et al 1984;Stangl and Baker 1984), allozymes (Avise et al 1974;Kilpatrick and Zimmerman 1975;Kilpatrick 1986, 1987;Rogers et al 2005;Selander et al 1971;Zimmerman et al 1975Zimmerman et al , 1978, cytogenetics (Greenbaum et al 1986a(Greenbaum et al , 1986bGreenbaum and Reed 1984;Hale 1986;Hale andGreenbaum 1988a, 1988b;McAllister and Greenbaum 1997;Sudman and Greenbaum 1990;Sudman et al 1989), speciation Zimmerman et al 1978), biogeography (Sullivan et al 1997), and many other areas of research. In addition, members of the genus Peromyscus are reservoirs for rodent-borne diseases such as Lyme disease (Levine et al 1985;Magnarelli et al 1988;Mather et al 1989;Rand et al 1993), hantaviruses (Childs et al 1994…”

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confidence: 99%

Toward a Molecular Phylogeny for Peromyscus: Evidence from Mitochondrial Cytochrome-bSequences

Bradley

Durish

Rogers

et al. 2007

Journal of Mammalogy

120

121

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One hundred DNA sequences from the mitochondrial cytochrome-b gene of 44 species of deer mice (Peromyscus (sensu stricto), 1 of Habromys, 1 of Isthmomys, 2 of Megadontomys, and the monotypic genera Neotomodon, Osgoodomys, and Podomys were used to develop a molecular phylogeny for Peromyscus. Phylogenetic analyses (maximum parsimony, maximum likelihood, and Bayesian inference) were conducted to evaluate alternative hypotheses concerning taxonomic arrangements (sensu stricto versus sensu lato) of the genus. In all analyses, monophyletic clades were obtained that corresponded to species groups proposed by previous authors; however, relationships among species groups generally were poorly resolved. The concept of the genus Peromyscus based on molecular data differed significantly from the most current taxonomic arrangement. Maximum-likelihood and Bayesian trees depicted strong support for a clade placing Habromys, Megadontomys, Neotomodon, Osgoodomys, and Podomys within Peromyscus. If Habromys, Megadontomys, Neotomodon, Osgoodomys, and Podomys are regarded as genera, then several species groups within Peromyscus (sensu stricto) should be elevated to generic rank. Isthmomys was associated with the genus Reithrodontomys; in turn this clade was sister to Baiomys, indicating a distant relationship of Isthmomys to Peromyscus. A formal taxonomic revision awaits synthesis of additional sequence data from nuclear markers together with inclusion of available allozymic and karyotypic data.

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p-Nitrosophenol Reduction by Liver Cytosol from ADH-Positive and -Negative Deermice (Peromyscus maniculatus)

Cited by 5 publications

References 0 publications

Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology

Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology

Multiple Adduction Reactions of Nitroso Sulfamethoxazole with Cysteinyl Residues of Peptides and Proteins: Implications for Hapten Formation

Toward a Molecular Phylogeny for Peromyscus: Evidence from Mitochondrial Cytochrome-bSequences

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