2008
DOI: 10.1016/j.bcp.2007.08.030
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Efficient oxidation of promutagenic hydroxymethylpyrenes by cDNA-expressed human alcohol dehydrogenase ADH2 and its inhibition by various agents

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Cited by 9 publications
(19 citation statements)
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“…Thus, it is necessary for kinetic analyses to physically separate the cDNA-expressed human ADH from the endogenous activity. In a preceding study we had partially purified human ADH2 expressed in S. typhimurium and demonstrated that this enzyme efficiently metabolises 1-HMP, 2-HMP and 4-HMP (Kollock et al, 2008). However, we also had found enhanced catalysis of the oxidation of 2-HMP by cytosolic fractions of bacteria expressing ADH3 and ADH4 bacteria compared to untransformed bacteria.…”
Section: Introductionmentioning
confidence: 79%
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“…Thus, it is necessary for kinetic analyses to physically separate the cDNA-expressed human ADH from the endogenous activity. In a preceding study we had partially purified human ADH2 expressed in S. typhimurium and demonstrated that this enzyme efficiently metabolises 1-HMP, 2-HMP and 4-HMP (Kollock et al, 2008). However, we also had found enhanced catalysis of the oxidation of 2-HMP by cytosolic fractions of bacteria expressing ADH3 and ADH4 bacteria compared to untransformed bacteria.…”
Section: Introductionmentioning
confidence: 79%
“…For the specification of susceptibility factors, we are striving to identify the human ADH forms involved in the detoxification of benzylic alcohols of PAHs. We succeeded expressing six forms in bacteria (Kollock et al, 2008); the remaining form, ADH5, was expressed in mammalian (Chinese hamster V79) cells, but failed to metabolise methylpyrene derivatives at significant rates (R. Kollock and H.R. Glatt, unpublished result).…”
Section: Introductionmentioning
confidence: 93%
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