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Спицын, В. А.; Nafikova, A. Kh.; Спицына, Н. Х.; Afanas'eva, I. S.

doi:10.1023/a:1016635219278

Russian Journal of Genetics

2001

DOI: 10.1023/a:1016635219278

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В. А. Спицын

A. Kh. Nafikova²,

Н. Х. Спицына

et al.

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Cited by 4 publications

(2 citation statements)

References 17 publications

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“…In humans, this enzyme (identical to esterase D) was highly expressed in liver and kidney, and its expression was stimulated by phenobarbital treatment (24). Genetic polymorphism of esterase D was discovered in various human populations, and the reduced enzymatic activity of this enzyme was found to be associated with the susceptibility to several pathological conditions (toxic liver cirrhosis, retinoblastoma, obesity, and autism) (25)(26)(27)(28).…”

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confidence: 99%

Molecular Basis of Formaldehyde Detoxification

González

Proudfoot

Brown

et al. 2006

Journal of Biological Chemistry

125

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The Escherichia coli genes frmB (yaiM) and yeiG encode two uncharacterized proteins that share 54% sequence identity and contain a serine esterase motif. We demonstrated that purified FrmB and YeiG have high carboxylesterase activity against the model substrates, p-nitrophenyl esters of fatty acids (C2-C6) and ␣-naphthyl acetate. However, both proteins had the highest hydrolytic activity toward S-formylglutathione, an intermediate of the ). In E. coli cells, the expression of frmB was stimulated 45-75 times by the addition of formaldehyde to the growth medium, whereas YeiG was found to be a constitutive enzyme. The simultaneous deletion of both frmB and yeiG genes was required to increase the sensitivity of the growth of E. coli cells to formaldehyde, suggesting that both FrmB and YeiG contribute to the detoxification of formaldehyde. Thus, FrmB and YeiG are S-formylglutathione hydrolases with a Ser-His-Asp catalytic triad involved in the detoxification of formaldehyde in E. coli.Formaldehyde is an extremely reactive chemical producing covalently cross-linked complexes with proteins and nucleic acids (1-3). It is a common environmental contaminant found in many industrial and medical products, as well as being endogenously produced in all living organisms as a result of metabolism (methionine, histamine, methanol, and methylamine), spontaneous dissociation of 5,10-mehylene tetrahydrofolate, or oxidative demethylation of DNA and RNA (4 -9). To prevent the lethal and mutagenic effects of formaldehyde, several repair mechanisms have evolved. Detoxification of formaldehyde can be carried out by enzymes like formaldehyde dismutase, methylformate synthase, or glutathioneindependent formaldehyde dehydrogenase (10 -12). However, these enzymes have been found in only a limited number of organisms, whereas a glutathione-dependent repair system appears to be widespread in nature and has been found in most prokaryotes (except for archaea) and all eukaryotes (7,(13)(14)(15).In this process (shown in Scheme 1), formaldehyde spontaneously reacts with GSH to produce S-hydroxymethylglutathione, which is then oxidized by formaldehyde dehydrogenase to S-formylglutathione. Finally, this compound is hydrolyzed to formate and GSH by S-formylglutathione hydrolase (FGH).2 These functionally related enzymes, formaldehyde dehydrogenase and FGH, also show genetic linkage, since their genes are adjacent in many bacterial genomes or even fused in some eukaryotes (16).Formaldehyde dehydrogenases (class III alcohol dehydrogenases) were extensively characterized both structurally and biochemically (17-20), whereas FGHs have received far less attention. Only three eukaryotic FGHs (from the human liver, Saccharomyces cerevisiae, and Arabidopsis thaliana) (21-23) have been purified and partially characterized, but the homologous enzyme from bacteria has not been yet purified. The FGH enzymes from yeasts and A. thaliana are not strictly specific to S-formylglutathione and also show significant carboxylesterase activity against model substrates ␣-n...

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confidence: 99%

Molecular Basis of Formaldehyde Detoxification

González

Proudfoot

Brown

et al. 2006

Journal of Biological Chemistry

125

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“…The ancient ancestors of this subfamily and those of the chimpanzee-man branch have diverged earlier (6.2-8.4 million years ago) than the ancestors of chimpanzee and man (4.6-6.2 million years ago), as it was determined by molecular genetic analysis [10]. Specific features of the human hairs has been con firmed by electrophoresis of their keratins, proteins that are different from those of other mammals, but to a lesser extent from hair keratins of the anthropoid apes (a sequential reduction of the keratin fractions is characteristic of both the apes and man) [11].…”

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confidence: 99%

Scanning electron microscopy of the hair medulla of orangutan, chimpanzee, and man

Чернова

2014

Dokl Biol Sci

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Health implications of α1-antitrypsin deficiency in Sub-Sahara African countries and their emigrants in Europe and the New World

Serres

Blanco

Fernández-Bustillo

2005

Genetics in Medicine

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Cited by 4 publications

References 17 publications

Molecular Basis of Formaldehyde Detoxification

Molecular Basis of Formaldehyde Detoxification

Scanning electron microscopy of the hair medulla of orangutan, chimpanzee, and man

Health implications of α1-antitrypsin deficiency in Sub-Sahara African countries and their emigrants in Europe and the New World

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