Substrate specificity of bovine liver formaldehyde dehydrogenase

Tayebeh Pourmotabbed, D. J. Creighton

Research output: Contribution to journalArticle

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Abstract

Formaldehyde dehydrogenases isolated from several different biological sources have been reported to catalyze the NAD+-dependent oxidative acylation of glutathione by methylglyoxal to form S-pyruvylglutathione, suggesting the involvement of this enzyme in the metabolism of methylglyoxal. However, formaldehyde dehydrogenase from bovine liver is found not to use methylglyoxal or related α-ketoaldehydes as substrates. Using methylglyoxal with the enzyme under conditions favoring the forward reaction did not result in the formation of S-pyruvylglutathione. Using independently synthesized S-pyruvylglutathione with the enzyme under conditions favoring the reverse reaction did not result in the production of methylglyoxal. In addition, methylglyoxal and several related α-ketoaldehydes did not exhibit detectable activity with formaldehyde dehydrogenase partially purified from human liver, contrary to a previous report. Some, if not all, past reports that methylglyoxal serves as a substrate for the dehydrogenase may be due to the demonstrated presence of contaminating formaldehyde in some commercially available preparations of methylglyoxal. In a related study, S-hydroxymethylglutathione, formed by pre-equilibrium addition of formaldehyde to glutathione, is concluded to be a direct substrate for the dehydrogenase. This follows from the observation that the catalytic turnover number of the enzyme in the forward direction exceeds by a factor of ~20 the first order rate constant for decomposition of S-hydroxymethylglutathione to glutathione and formaldehyde (k = 5.03 ± 0.30 min-1, pH 8, 25°C).

Original languageEnglish (US)
Pages (from-to)14240-14244
Number of pages5
JournalJournal of Biological Chemistry
Volume261
Issue number30
StatePublished - Dec 1 1986

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glutathione-independent formaldehyde dehydrogenase
Pyruvaldehyde
Substrate Specificity
Liver
Substrates
Formaldehyde
Glutathione
Enzymes
Oxidoreductases
Acylation
Metabolism
NAD

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Substrate specificity of bovine liver formaldehyde dehydrogenase. / Pourmotabbed, Tayebeh; Creighton, D. J.

In: Journal of Biological Chemistry, Vol. 261, No. 30, 01.12.1986, p. 14240-14244.

Research output: Contribution to journalArticle

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