Inhibition of Liver Alcohol Dehydrogenase by Amides.

Woronick, Charles L.; Frankenberg, Carl von; Sparrman, Berndt; Nielsen, Gerd; Nord, Hanna; Jart, Aage

doi:10.3891/acta.chem.scand.15-2062

Cited by 17 publications

(13 citation statements)

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“…Although a recent report indicating the existence of strong interactions between acrylamide and human serum albumin, monellin and ovalbumin (Blatt et al, 1986) has been disputed (Eftink and Ghiron, 1987), acrylamide is known to interact, usually as an inhibitor, with several enzymes. These include liver alcohol dehydrogenase (Woronick, 1961;Eftink and Selvidge, 1982), glucose 6-phosphate dehydrogenase (Harrison, 1974), acetylcholinesterase (Ngo, 1976), enolase and phosphofructokinase (Howland et al, 1980), trypsin and chymotrypsin (Eftink and Ghiron, 1987) and…”

Section: Introductionmentioning

confidence: 99%

The Interaction of Acrylamide With Glyceraldehyde‐3‐phosphate Dehydrogenase. Structural Modifications in the Enzyme Studied by Fluorescence Techniques

Örstan

Gafni

1990

Photochem & Photobiology

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The interaction of acrylamide with rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GPDH) has been investigated in Tris buffer, pH 7.5. When GPDH containing about 1 mol NAD per mol of tetramer is incubated with acrylamide (0.01-0.1 M), the tryptophan emission of GPDH, initially quenched by acrylamide, slowly increases to a value exceeding that recorded before the addition of acrylamide. This effect is not observed in apoenzyme solutions, indicating that the enhancement of fluorescence results from the dissociation of some NAD from the acrylamide treated GPDH. Acrylamide inactivates GPDH but 1 mM NAD protects the enzyme from inactivation. The addition of acrylamide to GPDH, labeled with fluorescein-5-isothiocyanate (GPDH-FITC) increases the fluorescence and decreases the polarization of fluorescein. The fluorescent sulfhydryl reagent N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine induces similar changes in the fluorescence properties of GPDH-FITC. This reagent, however, fails to react with GPDH preincubated with acrylamide and the titration of acrylamide treated GPDH with the sulfhydryl reagent 5,5'-dithiobis(2-nitrobenzoic acid) indicates the loss of up to 7 cysteine residues per tetramer. Acrylamide also decreases the heat stability of GPDH. Altogether, the data indicate that acrylamide covalently reacts with the active site cysteine residues of GPDH and subsequently induces a conformational change in the enzyme.

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Section: Introductionmentioning

confidence: 99%

The Interaction of Acrylamide With Glyceraldehyde‐3‐phosphate Dehydrogenase. Structural Modifications in the Enzyme Studied by Fluorescence Techniques

Örstan

Gafni

1990

Photochem & Photobiology

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“…Woronick and Johnson first identified an ATP-dependent CO2-fixing system in cell-free extracts from Aspergillus niger [35]. This novel reaction was postulated to result in the production of oxaloacetate from pyruvate, ATP and CO2.…”

Section: Pyruvate Carboxylasementioning

confidence: 99%

Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity

Lietzan

Maurice

2014

Archives of Biochemistry and Biophysics

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“…The resultant information has illuminated their mode of action, a subject which has long received careful attention through kinetic studies (65,67,91,118,121,122).…”

Section: H Mechanisms Of Inhibitionmentioning

confidence: 99%