Diacetyl and related flavorant α-Diketones: Biotransformation, cellular interactions, and respiratory-tract toxicity

Toxicology

Volumn 388, Issue , 2017, Pages 21-29

  Anders, M W ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

Acids and bases; Biotransformation; Covalent adduct formation; Diacetyl; Hard and soft; Quantum chemical methodology; diketones

Indexed keywords

1,2 DICARBONYL DERIVATIVE; 2,3 BUTANEDIONE; ACID; AKR1B PROTEIN; AKR1C PROTEIN; ALDEHYDE REDUCTASE; ALDO KETO REDUCTASE; ARGININE; BASE; GUANINE; LYSINE; OXIDOREDUCTASE; SDR24C1 PROTEIN; SDR25C PROTEIN; SHORT CHAIN DEHYDROGENASE REDUCTASE; UNCLASSIFIED DRUG; XYLULOSE REDUCTASE; FLAVORING AGENT; KETONE;

ARTICLE; BIOTRANSFORMATION; CELL FUNCTION; CELL INTERACTION; CHEMICAL REACTION; ENOLIZATION; ENZYME ACTIVITY; ENZYMOLOGY; HUMAN; HYDRATION; IN VIVO STUDY; METABOLISM; NONHUMAN; NUCLEOPHILICITY; PRIORITY JOURNAL; PROTEIN FAMILY; REACTION ANALYSIS; RESPIRATORY TRACT DISEASE; RESPIRATORY TRACT INJURY; RESPIRATORY TRACT TOXICITY; TOXICITY; ADVERSE EFFECTS; ANIMAL; CHEMICALLY INDUCED; CHEMISTRY; OCCUPATIONAL DISEASE; OCCUPATIONAL EXPOSURE;

ANIMALS; DIACETYL; FLAVORING AGENTS; HUMANS; KETONES; OCCUPATIONAL DISEASES; OCCUPATIONAL EXPOSURE; RESPIRATORY TRACT DISEASES;

EID: 85012893216     PISSN: 0300483X     EISSN: 18793185     Source Type: Journal    
DOI: 10.1016/j.tox.2017.02.002     Document Type: Article

References (146)

1. Akpinar-Elci, M., et al. Bronchiolitis obliterans syndrome in popcorn production plant workers. Eur. Respir. J. 24 (2004), 298–302.
2. Allen, J.G., et al. Flavoring chemicals in E-cigarettes: diacetyl, 2,3-pentanedione, and acetoin in a sample of 51 products including fruit-, candy-, and cocktail-flavored E-cigarettes. Environ. Health Perspect. 124 (2016), 733–739.
3. Anders, M.W., Bioactivation of Foreign Compounds. 1985, Academic Press, Orlando.
4. Anderson, S.E., et al. Evaluation of the hypersensitivity potential of alternative butter flavorings. Food Chem. Toxicol. 62 (2013), 373–381.
5. Aptula, A.O., Roberts, D.W., Mechanistic applicability domains for nonanimal-based prediction of toxicological end points: general principles and application to reactive toxicity. Chem. Res. Toxicol. 19 (2006), 1097–1105.
6. Bailey, R.L., et al. Respiratory morbidity in a coffee processing workplace with sentinel obliterative bronchiolitis cases. Am. J. Ind. Med. 58 (2015), 1235–1245.
7. Barrington-Trimis, J.L., et al. Flavorings in electronic cigarettes: an unrecognized respiratory health hazard?. JAMA 312 (2014), 2493–2494.
8. Barski, O.A., et al. The aldo-keto reductase superfamily and its role in drug metabolism and detoxification. Drug Metab. Rev. 40 (2008), 553–624.
9. Bell, R.P., McDougall, A.O., Hydration equilibriums of some aldehydes and ketones. Trans. Faraday Soc. 56 (1960), 1281–1285.
10. Bhatia, C., et al. Towards a systematic analysis of human short-chain dehydrogenases/reductases (SDR): ligand identification and structure-activity relationships. Chem. – Biol. Interact. 234 (2015), 114–125.
11. Björnestedt, R., et al. Functional significance of arginine 15 in the active site of human class Alpha glutathione transferase A1-1. J. Mol. Biol. 247 (1995), 765–773.
12. Bjeldanes, L.F., Chew, H., Mutagenicity of 1,2-dicarbonyl compounds: maltol, kojic acid, diacetyl and related substances. Mutat. Res. Genet. Toxicol. 67 (1979), 367–371.
13. Boylstein, R., Identification of diacetyl substitutes at a microwave popcorn production plant. J. Occup. Environ. Hyg. 9 (2012), D33–D34.
14. Burgos, J., Martin, R., Purification and some properties of diacetyl reductase from beef liver. Biochim. Biophys. Acta Enzymol. 268 (1972), 261–270.
15. Buschmann, H.-J., et al. The reversible hydration of carbonyl compounds in aqueous solution: part I. The keto/gem-diol equilibrium. Ber. Bunsen Ges. 84 (1980), 41–44.
16. Calam, E., et al. Biocatalytic production of α-hydroxy ketones and vicinal diols by yeast and human aldo-keto reductases. Chem. – Biol. Interact. 202 (2013), 195–203.
17. Cao, D., et al. Identification and characterization of a novel human aldose reductase-like gene. J. Biol. Chem. 273 (1998), 11429–11435.
18. Carbone, V., et al. Structure-based discovery of human L-xylulose reductase inhibitors from database screening and molecular docking. Bioorg. Med. Chem. 13 (2005), 301–312.
19. Chattaraj, P.K., et al. Electrophilicity index. Chem. Rev. 106 (2006), 2065–2091.
20. Chen, G., Chen, X., Arginine residues in the active site of human phenol sulfotransferase (SULT1A1). J. Biol. Chem. 278 (2003), 36358–36364.
21. Clark, S., Winter, C.K., Diacetyl in foods: a review of safety and sensory characteristics. Compr. Rev. Food Sci. Food Saf. 14 (2015), 634–643.
22. Codreanu, S.G., et al. Global analysis of protein damage by the lipid electrophile 4-hydroxy-2-nonenal. Mol. Cell. Proteomics 8 (2009), 670–680.
23. Codreanu, S.G., et al. Alkylation damage by lipid electrophiles targets functional protein systems. Mol. Cell. Proteomics 11 (2014), 849–859.
24. Connor, R.E., et al. Targeted protein capture for analysis of electrophile-protein adducts. Phillips, I.R., Shephard, E.A., Ortiz de Montellano, P.R., (eds.) Cytochrome P450 Protocols, 2013, Springer Protocols, New York, 163–176.
25. Couri, D., Milks, M., Toxicity and metabolism of the neurotoxic hexacarbons n-hexane 2-hexanone, and 2,5-hexanedione. Annu. Rev. Pharmacol. Toxicol. 22 (1982), 145–166.
26. Cummings, K.J., et al. Respiratory symptoms and lung function abnormalities related to work at a flavouring manufacturing facility. Occup. Environ. Med. 71 (2014), 549–554.
27. Dawson, J., Hullin, R.P., Metabolism of acetoin. I. The formation and utilization of acetoin and butane-2:3-diol in the decerebrated cat. Biochem. J. 57 (1954), 177–180.
28. Day, G., et al. Identification and measurement of diacetyl substitutes in dry bakery mix production. J. Occup. Environ. Hyg. 8 (2011), 93–103.
29. DeCaprio, A.P., Fowke, J.H., Limited and selective adduction of carboxyl-terminal lysines in the high molecular weight neurofilament proteins by 2,5-hexanedione in vitro. Brain Res. 586 (1992), 219–228.
30. DeCaprio, A.P., et al. Covalent binding of a neurotoxic n-hexane metabolite: conversion of primary amines to substituted pyrrole adducts by 2,5-hexanedione. Toxicol. Appl. Pharmacol. 65 (1982), 440–450.
31. Dennehy, M.K., et al. Cytosolic and nuclear protein targets of thiol-reactive electrophiles. Chem. Res. Toxicol. 19 (2006), 20–29.
32. Dorado, L., et al. A contribution to the study of the structure-mutagenicity relationship for α-dicarbonyl compounds using the Ames test. Mutat. Res. Fundam. Mol. Mech. Mutagen. 269 (1992), 301–306.
33. Duling, M.G., et al. Environmental characterization of a coffee processing workplace with obliterative bronchiolitis in former workers. J. Occup. Environ. Hyg. 13 (2016), 770–781.
34. El-Kabbani, O., et al. Structure of the tetrameric form of human L-xylulose reductase: probing the inhibitor-binding site with molecular modeling and site-directed mutagenesis. Proteins 60 (2005), 424–432.
35. Endo, S., et al. Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10. Bioorg. Med. Chem. 18 (2010), 2485–2490.
36. Endo, S., et al. Selective inhibition of the tumor marker AKR1B10 by antiinflammatory N-phenylanthranilic acids and glycyrrhetic acid. Biol. Pharm. Bull. 33 (2010), 886–890.
37. Endo, S., et al. Cloning and characterization of four rabbit aldo-keto reductases featuring broad substrate specificity for xenobiotic and endogenous carbonyl compounds: relationship with multiple forms of drug ketone reductases. Drug Metab. Dispos. 42 (2014), 803–812.
38. Endo, S., et al. Human dehydrogenase/reductase (SDR family) member 11 is a novel type of 17β-hydroxysteroid dehydrogenase. Biochem. Biophy. Res. Commun. 472 (2016), 231–236.
39. Enoch, S.J., Cronin, M.T., A review of the electrophilic reaction chemistry involved in covalent DNA binding. Crit. Rev. Toxicol. 40 (2010), 728–748.
40. Enoch, S.J., et al. Electrophilic reaction chemistry of low molecular weight respiratory sensitizers. Chem. Res. Toxicol. 22 (2009), 1447–1453.
41. Enoch, S.J., The use of frontier molecular orbital calculations in predictive reactive toxicology. Cronin, M., Madden, J.C., (eds.) Silico Toxicology: Principles and Applications, 2010, Royal Society of Chemistry, Cambridge, 193–209.
42. Fedan, J.S., et al. Popcorn worker's lung: in vitro exposure to diacetyl, an ingredient in microwave popcorn butter flavoring, increases reactivity to methacholine. Toxicol. Appl. Pharmacol. 215 (2006), 17–22.
43. 1/N mice. Chem. – Biol. Interact. 227 (2015), 112–119.
44. Fidanza, N.G., et al. Conformational and topological analysis of the charge density in guanine-(-dicarbonyl adducts at AM1 level. J. Mol. Struct.: THEOCHEM 504 (2000), 59–67.
45. Flake, G.P., Morgan, D.L., Pathology of diacetyl and 2,3-pentanedione airway lesions in a rat model of obliterative bronchiolitis. Toxicology, 2016, 10.1016/j.tox.2016.10.013.
46. Foster, M.W., et al. Proteomic analysis of primary human airway epithelial cells exposed to the respiratory toxicant diacetyl. J. Proteome Res., 2016, 10.1021/acs.jproteome.6b00672.
47. Gabriel, M.A., et al. Metabolism of acetoin in mammalian liver slices and extracts. Interconversion with butane-2, 3-diol and biacetyl. Biochem. J. 124 (1971), 793–800.
48. 2 in intact animals and in liver mince preparation. Comp. Biochem. Physiol. Part B: Biochem. Mol. Biol. 41 (1972), 493–502.
49. Gabrielli, F., et al. A nuclear protein, synthesized in growth-arrested human hepatoblastoma cells, is a novel member of the short-chain alcohol dehydrogenase family. Eur. J. Biochem. 232 (1995), 473–477.
50. Galligan, J.J., et al. Stable histone adduction by 4-oxo-2-nonenal: a potential link between oxidative stress and epigenetics. J. Am. Chem. Soc. 136 (2014), 11864–11866.
51. Galligan, J.J., et al. Quantitative analysis and discovery of lysine and arginine modifications (QuARKMod). Anal. Chem., 2016, 10.1021/acs.analchem.6b04105.
52. Greenzaid, P., et al. A nuclear magnetic resonance study of the reversible hydration of aliphatic aldehydes and ketones. I. Oxygen-17 and proton spectra and equilibrium constants. J. Am. Chem. Soc. 89 (1967), 749–756.
53. Grossberg, A.L., Pressman, D., Modification of arginine in the active sites of antibodies. Biochemistry 7 (1968), 272–279.
54. Hara, A., et al. Discrimination of multiforms of diacetyl reductase in hamster liver. Prog. Clin. Biol. Res. 174 (1985), 291–304.
55. Harden, A., Norris, D., The diacetyl reaction for proteins. J. Physiol. 42 (1911), 332–336.
56. Heinz, S., et al. Genomic organization of the human gene HEP27: alternative promoter usage in HepG2 cells and monocyte-derived dendritic cells. Genomics 79 (2002), 608–615.
57. Hinson, J.A., Roberts, D.W., Role of covalent and noncovalent interactions in cell toxicity: effects on proteins. Annu. Rev. Pharmacol. Toxicol. 32 (1992), 471–510.
58. Holden, V.K., Hines, S.E., Update on flavoring-induced lung disease. Curr. Opin. Pulm. Med. 22 (2016), 158–164.
59. Hooper, D.L., Nuclear magnetic resonance measurements of equilibria involving hydration and hemiacetal formation from some carbonyl compounds. J. Chem. Soc. B, 1967, 169–170.
60. Hu, X.-H., et al. (−)-Epigallocatechin-3-gallate, a potential inhibitor to human dicarbonyl/L-xylulose reductase. J. Biochem. 154 (2013), 167–175.
61. Hu, D., et al. Synthesis of 8-hydroxy-2-iminochromene derivatives as selective and potent inhibitors of human carbonyl reductase 1. Org. Biomol. Chem. 13 (2015), 7487–7499.
62. Hubbs, A.F., et al. Respiratory toxicologic pathology of inhaled diacetyl in Sprague-Dawley rats. Toxicol. Pathol. 36 (2008), 330–344.
63. Hubbs, A.F., et al. Respiratory and olfactory cytotoxicity of inhaled 2,3-pentanedione in Sprague-Dawley rats. Am. J. Pathol. 181 (2012), 829–844.
64. Hubbs, A.F., et al. Accumulation of ubiquitin and sequestosome-1 implicate protein damage in diacetyl-induced cytotoxicity. Am. J. Pathol. 186 (2016), 2887–2908.
65. Hyndman, D.J., Flynn, T.G., Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family. Biochim. Biophys. Acta Gene Struct. Expression 1399 (1998), 198–202.
66. Ishikura, S., et al. Molecular cloning, expression and tissue distribution of hamster diacetyl reductase. Identity with L-xylulose reductase. Chem. – Biol. Interact. 130-132 (2001), 879–889.
67. Jaramillo, P., et al. Definition of a nucleophilicity scale. J. Phys. Chem. A 110 (2006), 8181–8187.
68. Jin, Y., Penning, T.M., Aldo-keto reductases and bioactivation/detoxication. Annu. Rev. Pharmacol. Toxicol. 47 (2007), 263–292.
69. Kalgutkar, A.S., et al. A comprehensive listing of bioactivation pathways of organic functional groups. Curr. Drug Metab. 6 (2005), 161–225.
70. Kim, S.B., et al. Desmutagenic effect of α-dicarbonyl and α-hydroxycarbonyl compounds against mutagenic heterocyclic amines. Mutat. Res., Fundam. Mol. Mech. Mutagen. 177 (1987), 9–15.
71. Kreiss, K., et al. Clinical bronchiolitis obliterans in workers at a microwave-popcorn plant. N. Engl. J. Med. 347 (2002), 330–338.
72. Kreiss, K., Recognizing occupational effects of diacetyl: what can we learn from this history?. Toxicology, 2016, 10.1016/j.tox.2016.06.009.
73. Kung, J.-F.T., New caramel compound from coffee. J. Agr. Food Chem. 22 (1974), 494–496.
74. LoPachin, R.M., Barber, D.S., Synaptic cysteine sulfhydryl groups as targets of electrophilic neurotoxicants. Toxicol. Sci. 94 (2006), 240–255.
75. LoPachin, R.M., Gavin, T., Molecular mechanisms of aldehyde toxicity: a chemical perspective. Chem. Res. Toxicol. 27 (2014), 1081–1091.
76. LoPachin, R.M., Gavin, T., Toxic neuropathies: mechanistic insights based on a chemical perspective. Neurosci. Lett. 596 (2015), 78–83.
77. LoPachin, R.M., Gavin, T., Reactions of electrophiles with nucleophilic thiolate sites: relevance to pathophysiological mechanisms and remediation. Free Radical Res. 50 (2016), 195–205.
78. LoPachin, R.M., et al. Structure-toxicity analysis of type-2 alkenes: in vitro neurotoxicity. Toxicol. Sci. 95 (2007), 136–146.
79. LoPachin, R.M., et al. Neurotoxic mechanisms of electrophilic type-2 alkenes: soft-soft interactions described by quantum mechanical parameters. Toxicol. Sci. 98 (2007), 561–570.
80. LoPachin, R.M., et al. Application of the hard and soft, acids and bases (HSAB) theory to toxicant-target interactions. Chem. Res. Toxicol. 25 (2012), 239–251.
81. Lopachin, R.M., Decaprio, A.P., Protein adduct formation as a molecular mechanism in neurotoxicity. Toxicol. Sci. 86 (2005), 214–225.
82. Maeda, M., et al. D-Erythrulose reductase can also reduce diacetyl: further purification and characterization of D-erythrulose reductase from chicken liver. J. Biochem. 123 (1998), 602–606.
83. Maeda, M., et al. Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases. Protein Eng. 15 (2002), 611–617.
84. Marnett, L.J., et al. Naturally occurring carbonyl compounds are mutagens in Salmonella tester strain TA104. Mutat. Res. Fundam. Mol. Mech. Mutagen. 148 (1985), 25–34.
85. Martin, R., Burgos, J., Diacetyl reductase in animal tissues and its intracellular distribution. Biochim. Biophys. Acta Enzymol. 212 (1970), 356–358.
86. Mathews, J.M., et al. Reaction of the butter flavorant diacetyl (2, 3-butanedione) with N-α-acetylarginine: a model for epitope formation with pulmonary proteins in the etiology of obliterative bronchiolitis. J. Agric. Food Chem. 58 (2010), 12761–12768.
87. Matsunaga, T., et al. Multiplicity of mammalian reductases for xenobiotic carbonyl compounds. Drug Metab. Pharmacokinet. 21 (2006), 1–18.
88. Matsunaga, T., et al. Potent and selective inhibition of the tumor marker AKR1B10 by bisdemethoxycurcumin: probing the active site of the enzyme with molecular modeling and site-directed mutagenesis. Biochem. Biophys. Res. Commun. 389 (2009), 128–132.
89. Mekenyan, O.G., Veith, G.D., The electronic factor in QSAR MO-parameters, competing interactions, reactivity and toxicity. SAR QSAR Environ. Res. 2 (1994), 129–143.
90. Mendoza, V.L., Vachet, R.W., Probing protein structure by amino acid-specific covalent labeling and mass spectrometry. Mass Spectrom. Rev. 28 (2009), 785–815.
91. Mindnich, R.D., Penning, T.M., Aldo-keto reductase (AKR) superfamily: genomics and annotation. Hum. Genomics 3 (2009), 362–370.
92. Miyata, K., et al. Spectroscopic evidence of α,α-dihydroxy ketone in biacetyl aqueous solutions. Bull. Chem. Soc. Jpn. 62 (1989), 367–371.
93. Montgomery, J.A., et al. Metabolism of 2,3-butanediol stereoisomers in the perfused rat liver. J. Biol. Chem. 268 (1993), 20185–20190.
94. More, S.S., et al. The butter flavorant, diacetyl, forms a covalent adduct with 2-deoxyguanosine, uncoils DNA, and leads to cell death. J. Agric. Food Chem. 60 (2012), 3311–3317.
95. More, S.S., et al. The butter flavorant, diacetyl, exacerbates β-amyloid cytotoxicity. Chem. Res.Toxicol. 25 (2012), 2083–2091.
96. Morgan, D.L., et al. Respiratory toxicity of diacetyl in C57BL/6 mice. Toxicol. Sci. 103 (2008), 169–180.
97. Morgan, D.L., et al. Bronchial and bronchiolar fibrosis in rats exposed to 2,3-pentanedione vapors: implications for bronchiolitis obliterans in humans. Toxicol. Pathol. 40 (2012), 448–465.
98. Morgan, D.L., et al. Chemical reactivity and respiratory toxicity of the α-diketone flavoring agents: 2, 3-butanedione, 2, 3-pentanedione, and 2, 3-hexanedione. Toxicol. Pathol. 44 (2016), 763–783.
99. Morris, J.B., Hubbs, A.F., Inhalation dosimetry of diacetyl and butyric acid: two components of butter flavoring vapors. Toxicol. Sci. 108 (2009), 173–183.
100. NIOSH. 2016. DHHS (NIOSH) Publication No. 2016-111. Criteria for a recommended standard: occupational exposure to diacetyl and 2,3-pentanedione. By McKernan LT, Niemeier RT, Kreiss K, Hubbs A, Park R, Dankovic D, Dunn KH, Parker J, Fedan K, Streicher R, Fedan J, Garcia A, Whittaker C, Gilbert S, Nourian F, Galloway E, Smith R, Lentz TJ, Hirst D, Topmiller J, Curwin B. DHHS, CDC. https://www.cdc.gov/niosh/docs/2016-111/pdfs/2016-111-all.pdf.
101. Nakagawa, J., et al. Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney. J. Biol. Chem. 277 (2002), 17883–17891.
102. National Toxicology Program, Chemical Information Review Document for Artificial Butter Flavoring and Constituents. Diacetyl [CAS No. 431-03-8] and Acetoin [CAS No. 513-86-0]. 2007, National Institute of Environmental Health Sciences, Research Triangle Park.
103. Nemerya, N.S., et al. Arginine residues in the active centers of muscle pyruvate dehydrogenase. Biochem. Int. 8 (1984), 369–376.
104. Nemerya, N.S., et al. Chemical modification of the essential arginine residues of pyruvate dehydrogenase prevents its phosphorylation by kinase. FEBS Lett. 394 (1996), 96–98.
105. Noack, W.-E., An ab initio study of the keto-enol tautomerism. Theor. Chim. Acta 53 (1979), 101–119.
106. Oppermann, U., Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology. Annu. Rev. Pharmacol. Toxicol. 47 (2007), 293–322.
107. Otsuka, M., et al. A detoxication route for acetaldehyde: metabolism of diacetyl, acetoin, and 2,3-butanediol in liver homogenate and perfused liver of rats. J. Biochem. 119 (1996), 246–251.
108. Park, B.K., et al. Drug bioactivation and protein adduct formation in the pathogenesis of drug-induced toxicity. Chem. – Biol. Interact. 192 (2011), 30–36.
109. Parr, R.G., Pearson, R.G., Absolute hardness: companion parameter to absolute electronegativity. J. Am. Chem. Soc. 105 (1983), 7512–7516.
110. Parr, R.G., et al. Electrophilicity index. J. Am. Chem. Soc. 121 (1999), 1922–1924.
111. Pearson, R.G., Hard and soft acids and bases, HSAB, part 1: fundamental principles. J. Chem. Educ. 45 (1968), 581–587.
112. Pearson, R.G., Recent advances in the concept of hard and soft acids and bases. J. Chem. Educ., 64, 1987, 561.
113. Pearson, R.G., Hard and soft acids and bases – the evolution of a chemical concep. Coord. Chem. Rev. 100 (1990), 403–425.
114. Pellegrini, S., et al. A human short-chain dehydrogenase/reductase gene: structure, chromosomal localization, tissue expression and subcellular localization of its product. Biochim. Biophys. Acta Gene Struct. Expression 1574 (2002), 215–222.
115. Penning, T.M., Drury, J.E., Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Arch. Biochem. Biophys. 464 (2007), 241–250.
116. Penning, T.M., The aldo-keto reductases (AKRs): overview. Chem. – Biol. Interact. 234 (2015), 236–246.
117. Persson, B., Kallberg, Y., Classification and nomenclature of the superfamily of short-chain dehydrogenases/reductases (SDRs). Chem. – Biol. Interact. 202 (2013), 111–115.
118. Persson, B., et al. The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chem. – Biol. Interact. 178 (2009), 94–98.
119. Petrash, J.M., All in the family: aldose reductase and closely related aldo-keto reductases. Cell. Mol. Life Sci. 61 (2004), 737–749.
120. Pierce, J.S., et al. Diacetyl and 2,3-pentanedione exposures associated with cigarette smoking: implications for risk assessment of food and flavoring workers. Crit. Rev. Toxicol. 44 (2014), 420–435.
121. Poulose, A.J., Kolattukudy, P.E., Enzymatic reduction of phenylglyoxal and 2,3-butanedione two commonly used arginine-modifying reagents, by the ketoacyl reductase domain of fatty acid synthase. Int. J. Biochem. 18 (1986), 807–812.
122. Provecho, F., et al. Further purification and characterization of diacetyl reducing enzymes from beef liver. Int. J. Biochem. 16 (1984), 423–427.
123. Pumford, N.R., Halmes, N.C., Protein targets of xenobiotic reactive intermediates. Annu. Rev. Pharmacol. Toxicol. 37 (1997), 91–117.
124. Riordan, J.F., Functional arginyl residues in carboxypeptidase A: modification with butanedione. Biochemistry 12 (1973), 3915–3923.
125. Roberts, D.W., et al. Structure-activity relationships in the murine local lymph node assay for skin sensitization: α,β-diketones. Contact Dermatitis 41 (1999), 14–17.
126. Roberts, D.W., et al. Mechanistic applicability domains for non-animal based prediction of toxicological endpoints: QSAR analysis of the Schiff base applicability domain for skin sensitization. Chem. Res. Toxicol. 19 (2006), 1228–1233.
127. Rodríguez Mellado, J.M., Ruiz Montoya, M., Correlations between chemical reactivity and mutagenic activity against S. typhimurium TA100 for α-dicarbonyl compounds as a proof of the mutagenic mechanism. Mutat. Res. Fundam. Mol. Mech. Mutagen. 304 (1994), 261–264.
128. Rogers, K., Weber, B.H., Evidence for an essential role for arginyl residues for yeast phosphoglycerate kinase. Arch. Biochem. Biophys. 180 (1977), 19–25.
129. Sümegi, B., et al. Diacetyl: a new substrate in the overall reaction of the pyruvate dehydrogenase complex. Biochim. Biophys. Acta 705 (1982), 70–75.
130. Saraiva, M.A., et al. Non-enzymatic model glycation reactions – a comprehensive study of the reactivity of a modified arginine with aldehydic and diketonic dicarbonyl compounds by electrospray mass spectrometry. J. Mass Spectrom. 41 (2006), 755–770.
131. Saraiva, M.A., et al. Reactions of a modified lysine with aldehydic and diketonic dicarbonyl compounds: an electrospray mass spectrometry structure/activity study. J. Mass Spectrom. 41 (2006), 216–228.
132. Saraiva, M.A., et al. Mass spectrometric studies of the reaction of a blocked arginine with diketonic α-dicarbonyls. Amino Acids 48 (2016), 873–885.
133. Sawada, H., et al. Kinetic and structural properties of diacetyl reductase from hamster liver. J. Biochem. 98 (1985), 1349–1357.
134. Schwarzenbach, G., Wittwer, C., Über die Enolgehalte einfacher ketone. Helv. Chim. Acta 30 (1947), 669–674.
135. Shafqat, N., et al. Hep27, a member of the short-chain dehydrogenase/reductase family, is an NADPH-dependent dicarbonyl reductase expressed in vascular endothelial tissue. Cell. Mol. Life Sci. 63 (2006), 1205–1213.
136. Smania, A.M., Argaraña, C.E., Molecular cloning and characterization of a cDNA encoding a bovine butanediol dehydrogenase. Gene 197 (1997), 231–238.
137. Uehara, K., et al. Studies on D-tetrose metabolism. IV. Purification and some properties of D-erythrulose reductase from beef liver. J. Biochem. 75 (1974), 333–345.
138. Uetrecht, J., Bioactivation. Fisher, M.B., Lee, J.S., Obach, R.S., (eds.) Drug Metabolizing Enzymes, 2003, Cytochrome P450 and Other Enzymes in Drug Discovery and Development, Marcel DekkerNew York, 87–146.
139. Uetrecht, J., Evaluation of which reactive metabolite, if any, is responsible for a specific idiosyncratic reaction. Drug Metab. Rev. 38 (2006), 745–753.
140. Vallee, B.L., Riordan, J.F., Chemical approaches to the properties of active sites of enzymes. Annu. Rev. Biochem. 38 (1969), 733–794.
141. Vila, A., et al. Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives. Chem. Res. Toxicol. 21 (2008), 432–444.
142. Westerfield, W.W., Berg, R.L., Observations on the metabolism of acetoin. J. Biol. Chem. 148 (1943), 523–528.
143. Xia, C., et al. Chemical modification of GSH transferase P 1-1 confirms the presence of Arg-13, Lys-44 and one carboxylate group in the GSH-binding domain of the active site. Biochem. J. 293 (1993), 357–362.
144. Yankeelov, J.A. Jr., et al. A reagent for the modification of arginine residues under mild conditions. Fed. Proc. Fed. Amer. Soc. Exp. Biol., 25, 1966, 590.
145. Zakim, D., et al. Evidence for an active site arginine in UDP-glucuronyltransferase. J. Biol. Chem. 258 (1983), 6430–6434.
146. Zhang, J., et al. Modeling of toxicity-relevant electrophilic reactivity for guanine with epoxides: estimating the hard and soft acids and bases (HSAB) parameter as a predictor. Chem. Res. Toxicol. 29 (2016), 841–850.